Function of a retrotransposon nucleocapsid protein

References

• Eickbush TH, Jamburuthugoda VK. The diversity of retrotransposons and the properties of their reverse transcriptases. Virus Res 2009; 134:221 - 234
   Web of Science ®Google Scholar
• Symer DE, Boeke JD. Kurth R, Bannert N. An everlasting war dance between retrotransposons and their metazoan hosts. Retroviruses 2010; Norfolk, UK Caister Academic Press 1 - 34
   Google Scholar
• Beauregard A, Curcio MJ, Belfort M. The take and give between retrotransposable elements and their hosts. Annu Rev Genet 2008; 42:587 - 617
   Web of Science ®Google Scholar
• Bannert N, Fiebig U, Hohn O. Kurth R, Bannert N. Retroviral particles, proteins and genomes. Retroviruses 2010; Norfolk, UK Caister Academic Press 71 - 106
   Google Scholar
• Engelman A. Kurth R, Bannert N. Reverse transcription and uncoating. Retroviruses 2010; Norfolk, UK Caisert Academic press 129 - 160
   Google Scholar
• Cimarelli A, Darlix JL. Assembling the human immunodeficiency virus type 1. Cell Mol Life Sci 2002; 59:1166 - 1184
   PubMed Web of Science ®Google Scholar
• Bampi C, Jacquenet S, Lener D, Decimo D, Darlix JL. The chaperoning and assistance roles of the HIV-1 nucleocapsid protein in proviral DNA synthesis and maintenance. Int J Biochem Cell Biol 2004; 36:1668 - 1686
   PubMed Web of Science ®Google Scholar
• Mougel M, Houzet L, Darlix JL. When is it time for reverse transcription to start and go?. Retrovirology 2009; 6:24
   PubMed Web of Science ®Google Scholar
• Thomas JA, Gorelick RJ. Nucleocapsid protein function in early infection processes. Virus Res 2008; 134:39 - 63
   PubMed Web of Science ®Google Scholar
• Levin JG, Guo J, Rouzina I, Musier-Forsyth K. Nucleic acid chaperone activity of HIV-1 nucleocapsid protein: critical role in reverse transcription and molecular mechanism. Prog Nucleic Acid Res Mol Biol 2005; 80:217 - 286
   PubMed Web of Science ®Google Scholar
• Kurth R, Bannert N. Retroviruses 2010; Norfolk, UK Caister Academic Press
   Google Scholar
• Ganser-Pornillos BK, Yeager M, Sundquist WI. The structural biology of HIV assembly. Curr Opin Struct Biol 2008; 18:203 - 217
   PubMed Web of Science ®Google Scholar
• Scarlata S, Carter C. Role of HIV-1 Gag domains in viral assembly. Biochim Biophys Acta 2003; 1614:62 - 72
   PubMed Web of Science ®Google Scholar
• Wilk T, Fuller SD. Towards the structure of the human immunodeficiency virus: divide and conquer. Curr Opin Struct Biol 1999; 9:231 - 243
   PubMed Web of Science ®Google Scholar
• Linial ML, Eastman SW. Particle assembly and genome packaging. Curr Top Microbiol Immunol 2003; 277:89 - 110
   PubMed Web of Science ®Google Scholar
• Morita E, Sundquist WI. Retrovirus budding. Annu Rev Cell Dev Biol 2004; 20:395 - 425
   PubMed Web of Science ®Google Scholar
• Freed EO, Mouland AJ. The cell biology of HIV-1 and other retroviruses. Retrovirology 2006; 3:77
   PubMed Web of Science ®Google Scholar
• Yu SF, Sullivan MD, Linial ML. Evidence that the human foamy virus genome is DNA. J Virol 1999; 73:1565 - 1572
   PubMed Web of Science ®Google Scholar
• Dvorin JD, Malim MH. Intracellular trafficking of HIV-1 cores: journey to the center of the cell. Curr Top Microbiol Immunol 2003; 281:179 - 208
   PubMed Web of Science ®Google Scholar
• Voytas DF, Boeke JD. Craig NL, Craigie R, Gellert M, Lambowitz AM. Ty1 and Ty5 of Saccharomyces cerevisiae. Mobile DNA II 2002; Washington DC American Society for Microbiology 631 - 662
   Google Scholar
• Sandmeyer SB, Aye M, Menees TM. Ty3: a positionspecific gypsylike element in Saccharomyces cerevisiae 2002; Washington DC ASM Press
   Google Scholar
• Kim A, Terzian C, Santamaria P, Pelisson A, Purd'homme N, Bucheton A. Retroviruses in invertebrates: the gypsy retrotransposon is apparently an infectious retrovirus of Drosophila melanogaster. Proc Natl Acad Sci USA 1994; 91:1285 - 1289
   PubMed Web of Science ®Google Scholar
• Gao X, Rowley DJ, Gai X, Voytas DF. Ty5 gag mutations increase retrotransposition and suggest a role for hydrogen bonding in the function of the nucleocapsid zinc finger. J Virol 2002; 76:3240 - 3247
   PubMed Web of Science ®Google Scholar
• Kirchner J, Sandmeyer SB, Forrest DB. Transposition of a Ty3 GAG3-POL3 fusion mutant is limited by availability of capsid protein. J Virol 1992; 66:6081 - 6092
   PubMed Web of Science ®Google Scholar
• Farabaugh PJ, Zhao H, Vimaladithan A. A novel programed frameshift expresses the POL3 gene of retrotransposon Ty3 of yeast: frameshifting without tRNA slippage. Cell 1993; 74:93 - 103
   PubMed Web of Science ®Google Scholar
• Krausslich HG, Facke M, Heuser AM, Konvalinka J, Zentgraf H. The spacer peptide between human immunodeficiency virus capsid and nucleocapsid proteins is essential for ordered assembly and viral infectivity. J Virol 1995; 69:3407 - 3419
   PubMed Web of Science ®Google Scholar
• Craven RC, Leure-duPree AE, Erdie CR, Wilson CB, Wills JW. Necessity of the spacer peptide between CA and NC in the Rous sarcoma virus gag protein. J Virol 1993; 67:6246 - 6252
   PubMed Web of Science ®Google Scholar
• Zhang M. Ty3 virus-like particle morphogenesis and assembly 2007; Irvine, CA University of California, Irvine
   Google Scholar
• Kirchner J, Sandmeyer S. Proteolytic processing of Ty3 proteins is required for transposition. J Virol 1993; 67:19 - 28
   PubMed Web of Science ®Google Scholar
• Claypool JA, Malik HS, Eickbush TH, Sandmeyer SB. Ten-kilodalton domain in Ty3 Gag3-Pol3p between PR and RT is dispensable for Ty3 transposition. J Virol 2001; 75:1557 - 1560
   PubMed Web of Science ®Google Scholar
• Hansen LJ, Chalker DL, Orlinsky KJ, Sandmeyer SB. Ty3 GAG3 and POL3 genes encode the components of intracellular particles. J Virol 1992; 66:1414 - 1424
   PubMed Web of Science ®Google Scholar
• Orlinsky KJ, Sandmeyer SB. The Cys-His motif of Ty3 NC can be contributed by Gag3 or Gag3-Pol3 polyproteins. J Virol 1994; 68:4152 - 4166
   PubMed Web of Science ®Google Scholar
• Bilanchone VW, Claypool JA, Kinsey PT, Sandmeyer SB. Positive and negative regulatory elements control expression of the yeast retrotransposon Ty3. Genetics 1993; 134:685 - 700
   PubMed Web of Science ®Google Scholar
• Kinsey PT, Sandmeyer SB. Ty3 transposes in mating populations of yeast: a novel transposition assay for Ty3. Genetics 1995; 139:81 - 94
   PubMed Web of Science ®Google Scholar
• Hansen LJ, Chalker DL, Sandmeyer SB. Ty3, a yeast retrotransposon associated with tRNA genes, has homology to animal retroviruses. Mol Cell Biol 1988; 8:5245 - 5256
   PubMed Web of Science ®Google Scholar
• Beliakova-Bethell N, Beckham C, Giddings TH Jr, Winey M, Parker R, Sandmeyer S. Virus-like particles of the Ty3 retrotransposon assemble in association with P-body components. RNA 2006; 12:94 - 101
   PubMed Web of Science ®Google Scholar
• Campbell S, Vogt VM. In vitro assembly of virus-like particles with Rous sarcoma virus Gag deletion mutants: identification of the p10 domain as a morphological determinant in the formation of spherical particles. J Virol 1997; 71:4425 - 4435
   PubMed Web of Science ®Google Scholar
• Campbell S, Rein A. In vitro assembly properties of human immunodeficiency virus type 1 Gag protein lacking the p6 domain. J Virol 1999; 73:2270 - 2279
   PubMed Web of Science ®Google Scholar
• Zhang Y, Qian H, Love Z, Barklis E. Analysis of the assembly function of the human immunodeficiency virus type 1 gag protein nucleocapsid domain. J Virol 1998; 72:1782 - 1789
   PubMed Web of Science ®Google Scholar
• Muriaux D, Mirro J, Harvin D, Rein A. RNA is a structural element in retrovirus particles. Proc Natl Acad Sci USA 2001; 98:5246 - 5251
   PubMed Web of Science ®Google Scholar
• Wright ER, Schooler JB, Ding HJ, Kieffer C, Fillmore C, Sundquist WI, et al. Electron cryotomography of immature HIV-1 virions reveals the structure of the CA and SP1 Gag shells. EMBO J 2007; 26:2218 - 2226
   PubMed Web of Science ®Google Scholar
• Larsen LS, Zhang M, Beliakova-Bethell N, Bilanchone V, Lamsa A, Nagashima K, et al. Ty3 capsid mutations reveal early and late functions of the amino-terminal domain. J Virol 2007; 81:6957 - 6972
   PubMed Web of Science ®Google Scholar
• Zhang M, Larsen LS, Irwin B, Bilanchone V, Sandmeyer S. Two-hybrid analysis of Ty3 capsid subdomain interactions. Mob DNA 2010; 1:14
   PubMedGoogle Scholar
• Larsen LS, Beliakova-Bethell N, Bilanchone V, Zhang M, Lamsa A, Dasilva R, et al. Ty3 nucleocapsid controls localization of particle assembly. J Virol 2008; 82:2501 - 2514
   Google Scholar
• Kuznetsov YG, Zhang M, Menees TM, McPherson A, Sandmeyer S. Investigation by atomic force microscopy of the structure of Ty3 retrotransposon particles. J Virol 2005; 79:8032 - 8045
   PubMed Web of Science ®Google Scholar
• Klein KC, Reed JC, Lingappa JR. Intracellular destinies: degradation, targeting, assembly and endocytosis of HIV Gag. AIDS Rev 2007; 9:150 - 161
   PubMed Web of Science ®Google Scholar
• Bieniasz PD. The cell biology of HIV-1 virion genesis. Cell Host Microbe 2009; 5:550 - 558
   PubMed Web of Science ®Google Scholar
• Butsch M, Boris-Lawrie K. Destiny of unspliced retroviral RNA: ribosome and/or virion?. J Virol 2002; 76:3089 - 3094
   PubMed Web of Science ®Google Scholar
• Cochrane AW, McNally MT, Mouland AJ. The retrovirus RNA trafficking granule: from birth to maturity. Retrovirology 2006; 3:18
   Google Scholar
• Malim MH, Emerman M. HIV-1 accessory proteins—ensuring viral survival in a hostile environment. Cell Host Microbe 2008; 3:388 - 398
   PubMed Web of Science ®Google Scholar
• Nekhai S, Jeang KT. Transcriptional and post-transcriptional regulation of HIV-1 gene expression: role of cellular factors for Tat and Rev. Future Microbiol 2006; 1:417 - 426
   PubMed Web of Science ®Google Scholar
• Bray M, Prasad S, Dubay JW, Hunter E, Jeang KT, Rekosh D, et al. A small element from the Mason-Pfizer monkey virus genome makes human immunodeficiency virus type 1 expression and replication Rev-independent. Proc Natl Acad Sci USA 1994; 91:1256 - 1260
   PubMed Web of Science ®Google Scholar
• Levin JG, Rosenak MJ. Synthesis of murine leukemia virus proteins associated with virions assembled in actinomycin D-treated cells: evidence for persistence of viral messenger RNA. Proc Natl Acad Sci USA 1976; 73:1154 - 1158
   PubMed Web of Science ®Google Scholar
• Flynn JA, Telesnitsky A. Two distinct Moloney murine leukemia virus RNAs produced from a single locus dimerize at random. Virology 2006; 344:391 - 400
   Google Scholar
• Butterfield-Gerson KL, Scheifele LZ, Ryan EP, Hopper AK, Parent LJ. Importin-beta family members mediate alpharetrovirus gag nuclear entry via interactions with matrix and nucleocapsid. J Virol 2006; 80:1798 - 1806
   PubMed Web of Science ®Google Scholar
• Gudleski N, Flanagan JM, Ryan EP, Bewley MC, Parent LJ. Directionality of nucleocytoplasmic transport of the retroviral gag protein depends on sequential binding of karyopherins and viral RNA. Proc Natl Acad Sci USA 2010; 107:9358 - 9363
   PubMed Web of Science ®Google Scholar
• Swanson CM, Puffer BA, Ahmad KM, Doms RW, Malim MH. Retroviral mRNA nuclear export elements regulate protein function and virion assembly. EMBO J 2004; 23:2632 - 2640
   PubMed Web of Science ®Google Scholar
• Anderson EC, Lever AM. Human immunodeficiency virus type 1 Gag polyprotein modulates its own translation. J Virol 2006; 80:10478 - 10486
   Google Scholar
• Berkowitz RD, Ohagen A, Hoglund S, Goff SP. Retroviral nucleocapsid domains mediate the specific recognition of genomic viral RNAs by chimeric Gag polyproteins during RNA packaging in vivo. J Virol 1995; 69:6445 - 6456
   PubMed Web of Science ®Google Scholar
• Zhang Y, Barklis E. Nucleocapsid protein effects on the specificity of retrovirus RNA encapsidation. J Virol 1995; 69:5716 - 5722
   PubMed Web of Science ®Google Scholar
• D'Souza V, Summers MF. How retroviruses select their genomes. Nat Rev Microbiol 2005; 3:643 - 655
   PubMed Web of Science ®Google Scholar
• D'Souza V, Summers MF. Structural basis for packaging the dimeric genome of Moloney murine leukaemia virus. Nature 2004; 431:586 - 590
   PubMed Web of Science ®Google Scholar
• De Guzman RN, Wu ZR, Stalling CC, Pappalardo L, Borer PN, Summers MF. Structure of the HIV-1 nucleocapsid protein bound to the SL3 psi-RNA recognition element. Science 1998; 279:384 - 388
   PubMed Web of Science ®Google Scholar
• Johnson MC, Scobie HM, Ma YM, Vogt VM. Nucleic acid-independent retrovirus assembly can be driven by dimerization. J Virol 2002; 76:11177 - 11185
   PubMed Web of Science ®Google Scholar
• Larson DR, Ma YM, Vogt VM, Webb WW. Direct measurement of Gag-Gag interaction during retrovirus assembly with FRET and fluorescence correlation spectroscopy. J Cell Biol 2003; 162:1233 - 1244
   Google Scholar
• Jouvenet N, Bieniasz PD, Simon SM. Imaging the biogenesis of individual HIV-1 virions in live cells. Nature 2008; 454:236 - 240
   Google Scholar
• Perlman M, Resh MD. Identification of an intracellular trafficking and assembly pathway for HIV-1 gag. Traffic 2006; 7:731 - 745
   PubMed Web of Science ®Google Scholar
• Resh MD. Intracellular trafficking of HIV-1 Gag: how Gag interacts with cell membranes and makes viral particles. AIDS Rev 2005; 7:84 - 91
   PubMed Web of Science ®Google Scholar
• Dooher JE, Schneider BL, Reed JC, Lingappa JR. Host ABCE1 is at plasma membrane HIV assembly sites and its dissociation from Gag is linked to subsequent events of virus production. Traffic 2007; 8:195 - 211
   PubMed Web of Science ®Google Scholar
• Basyuk E, Boulon S, Skou Pedersen F, Bertrand E, Vestergaard Rasmussen S. The packaging signal of MLV is an integrated module that mediates intracellular transport of genomic RNAs. J Mol Biol 2005; 354:330 - 339
   PubMed Web of Science ®Google Scholar
• Poole E, Strappe P, Mok HP, Hicks R, Lever AM. HIV-1 Gag-RNA interaction occurs at a perinuclear/centrosomal site; analysis by confocal microscopy and FRET. Traffic 2005; 6:741 - 755
   PubMed Web of Science ®Google Scholar
• Grigorov B, Decimo D, Smagulova F, Pechoux C, Mougel M, Muriaux D, et al. Intracellular HIV-1 Gag localization is impaired by mutations in the nucleocapsid zinc fingers. Retrovirology 2007; 4:54
   PubMed Web of Science ®Google Scholar
• Levesque K, Halvorsen M, Abrahamyan L, Chatel-Chaix L, Poupon V, Gordon H, et al. Trafficking of HIV-1 RNA is mediated by heterogeneous nuclear ribonucleoprotein A2 expression and impacts on viral assembly. Traffic 2006; 7:1177 - 1193
   PubMedGoogle Scholar
• Chen C, Jin J, Rubin M, Huang L, Sturgeon T, Weixel KM, et al. Association of gag multimers with filamentous actin during equine infectious anemia virus assembly. Curr HIV Res 2007; 5:315 - 323
   PubMed Web of Science ®Google Scholar
• Krogstad P, Geng YZ, Rey O, Canon J, Ibarrondo FJ, Ackerson B, et al. Human immunodeficiency virus nucleocapsid protein polymorphisms modulate the infectivity of RNA packaging mutants. Virology 2002; 294:282 - 288
   PubMed Web of Science ®Google Scholar
• Liu B, Dai R, Tian CJ, Dawson L, Gorelick R, Yu XF. Interaction of the human immunodeficiency virus type 1 nucleocapsid with actin. J Virol 1999; 73:2901 - 2908
   PubMed Web of Science ®Google Scholar
• Wilk T, Gowen B, Fuller SD. Actin associates with the nucleocapsid domain of the human immunodeficiency virus Gag polyprotein. J Virol 1999; 73:1931 - 1940
   PubMedGoogle Scholar
• Hong S, Choi G, Park S, Chung AS, Hunter E, Rhee SS. Type D retrovirus Gag polyprotein interacts with the cytosolic chaperonin TRiC. J Virol 2001; 75:2526 - 2534
   PubMed Web of Science ®Google Scholar
• Lingappa JR, Dooher JE, Newman MA, Kiser PK, Klein KC. Basic residues in the nucleocapsid domain of Gag are required for interaction of HIV-1 gag with ABCE1 (HP68), a cellular protein important for HIV-1 capsid assembly. J Biol Chem 2006; 281:3773 - 3784
   PubMed Web of Science ®Google Scholar
• Malagon F, Jensen TH. The T body, a new cytoplasmic RNA granule in Saccharomyces cerevisiae. Mol Cell Biol 2008; 28:6022 - 6032
   PubMedGoogle Scholar
• Dutko JA, Kenny AE, Gamache ER, Curcio MJ. 5′ to 3′ mRNA decay factors colocalize with Ty1 gag and human APOBEC3G and promote Ty1 retrotransposition. J Virol 2010; 84:5052 - 5066
   PubMed Web of Science ®Google Scholar
• Checkley MA, Nagashima K, Lockett SJ, Nyswaner KM, Garfinkel DJ. P-body components are required for Ty1 retrotransposition during assembly of retrotransposition-competent virus-like particles. Mol Cell Biol 2010; 30:382 - 398
   PubMedGoogle Scholar
• Griffith JL, Coleman LE, Raymond AS, Goodson SG, Pittard WS, Tsui C, et al. Functional genomics reveals relationships between the retrovirus-like Ty1 element and its host Saccharomyces cerevisiae. Genetics 2003; 164:867 - 879
   PubMed Web of Science ®Google Scholar
• Irwin B, Aye M, Baldi P, Beliakova-Bethell N, Cheng H, Dou Y, et al. Retroviruses and yeast retrotransposons use overlapping sets of host genes. Genome Res 2005; 15:641 - 654
   PubMed Web of Science ®Google Scholar
• Balagopal V, Parker R. Polysomes, P bodies and stress granules: states and fates of eukaryotic mRNAs. Curr Opin Cell Biol 2009; 21:403 - 408
   PubMed Web of Science ®Google Scholar
• Nissan T, Parker R. Analyzing P-bodies in Saccharomyces cerevisiae. Methods Enzymol 2008; 448:507 - 520
   PubMed Web of Science ®Google Scholar
• Buchan JR, Parker R. Eukaryotic stress granules: the ins and outs of translation. Mol Cell 2009; 36:932 - 941
   PubMed Web of Science ®Google Scholar
• Buchan JR, Muhlrad D, Parker R. P bodies promote stress granule assembly in Saccharomyces cerevisiae. J Cell Biol 2008; 183:441 - 455
   PubMed Web of Science ®Google Scholar
• Hu W, Sweet TJ, Chamnongpol S, Baker KE, Coller J. Co-translational mRNA decay in Saccharomyces cerevisiae. Nature 2009; 461:225 - 229
   PubMed Web of Science ®Google Scholar
• Hoyle NP, Castelli LM, Campbell SG, Holmes LE, Ashe MP. Stress-dependent relocalization of translationally primed mRNPs to cytoplasmic granules that are kinetically and spatially distinct from P-bodies. J Cell Biol 2007; 179:65 - 74
   PubMed Web of Science ®Google Scholar
• Kedersha N, Anderson P. Mammalian stress granules and processing bodies. Methods Enzymol 2007; 431:61 - 81
   PubMed Web of Science ®Google Scholar
• Kapp LD, Lorsch JR. The molecular mechanics of eukaryotic translation. Annu Rev Biochem 2004; 73:657 - 704
   PubMed Web of Science ®Google Scholar
• Coller J, Parker R. General translational repression by activators of mRNA decapping. Cell 2005; 122:875 - 886
   PubMed Web of Science ®Google Scholar
• Coller JM, Tucker M, Sheth U, Valencia-Sanchez MA, Parker R. The DEAD box helicase, Dhh1p, functions in mRNA decapping and interacts with both the decapping and deadenylase complexes. RNA 2001; 7:1717 - 1727
   PubMedGoogle Scholar
• Gorelick RJ, Henderson LE, Hanser JP, Rein A. Point mutants of Moloney murine leukemia virus that fail to package viral RNA: evidence for specific RNA recognition by a “zinc finger-like” protein sequence. Proc Natl Acad Sci USA 1988; 85:8420 - 8424
   PubMed Web of Science ®Google Scholar
• Dupraz P, Oertle S, Meric C, Damay P, Spahr PF. Point mutations in the proximal Cys-His box of Rous sarcoma virus nucleocapsid protein. J Virol 1990; 64:4978 - 4987
   PubMed Web of Science ®Google Scholar
• Dorfman T, Luban J, Goff SP, Haseltine WA, Gottlinger HG. Mapping of functionally important residues of a cysteine-histidine box in the human immunodeficiency virus type 1 nucleocapsid protein. J Virol 1993; 67:6159 - 6169
   PubMed Web of Science ®Google Scholar
• Beliakova-Bethell N, Terry LJ, Bilanchone V, DaSilva R, Nagashima K, Wente SR, et al. Ty3 nuclear entry is initiated by viruslike particle docking on GLFG nucleoporins. J Virol 2009; 83:11914 - 11925
   PubMed Web of Science ®Google Scholar
• Scheifele LZ, Garbitt RA, Rhoads JD, Parent LJ. Nuclear entry and CRM1-dependent nuclear export of the Rous sarcoma virus Gag polyprotein. Proc Natl Acad Sci USA 2002; 99:3944 - 3949
   PubMed Web of Science ®Google Scholar
• Garbitt-Hirst R, Kenney SP, Parent LJ. Genetic evidence for a connection between Rous sarcoma virus gag nuclear trafficking and genomic RNA packaging. J Virol 2009; 83:6790 - 6797
   PubMed Web of Science ®Google Scholar
• Rey O, Canon J, Krogstad P. HIV-1 Gag protein associates with F-actin present in microfilaments. Virology 1996; 220:530 - 534
   Google Scholar
• Gladnikoff M, Shimoni E, Gov NS, Rousso I. Retroviral assembly and budding occur through an actin-driven mechanism. Biophys J 2009; 97:2419 - 2428
   PubMed Web of Science ®Google Scholar
• Mouland AJ, Mercier J, Luo M, Bernier L, DesGroseillers L, Cohen EA. The double-stranded RNA-binding protein Staufen is incorporated in human immunodeficiency virus type 1: evidence for a role in genomic RNA encapsidation. J Virol 2000; 74:5441 - 5451
   PubMed Web of Science ®Google Scholar
• Chatel-Chaix L, Boulay K, Mouland AJ, Desgroseillers L. The host protein Staufen1 interacts with the Pr55Gag zinc fingers and regulates HIV-1 assembly via its N-terminus. Retrovirology 2008; 5:41
   PubMed Web of Science ®Google Scholar
• Bacharach E, Gonsky J, Alin K, Orlova M, Goff SP. The carboxy-terminal fragment of nucleolin interacts with the nucleocapsid domain of retroviral gag proteins and inhibits virion assembly. J Virol 2000; 74:11027 - 11039
   PubMed Web of Science ®Google Scholar
• Popov S, Popova E, Inoue M, Gottlinger HG. Human immunodeficiency virus type 1 Gag engages the Bro1 domain of ALIX/AIP1 through the nucleocapsid. J Virol 2008; 82:1389 - 1398
   PubMed Web of Science ®Google Scholar
• Dussupt V, Javid MP, Abou-Jaoude G, Jadwin JA, de La Cruz J, Nagashima K, et al. The nucleocapsid region of HIV-1 Gag cooperates with the PTAP and LYPXnL late domains to recruit the cellular machinery necessary for viral budding. PLoS Pathog 2009; 5:1000339
   Web of Science ®Google Scholar
• Popova E, Popov S, Gottlinger HG. Human immunodeficiency virus type 1 nucleocapsid p1 confers ESCRT pathway dependence. J Virol 2010; 84:6590 - 6597
   PubMed Web of Science ®Google Scholar
• Luo K, Liu B, Xiao Z, Yu Y, Yu X, Gorelick R, et al. Amino-terminal region of the human immunodeficiency virus type 1 nucleocapsid is required for human APOBEC3G packaging. J Virol 2004; 78:11841 - 11852
   PubMed Web of Science ®Google Scholar
• Alce TM, Popik W. APOBEC3G is incorporated into virus-like particles by a direct interaction with HIV-1 Gag nucleocapsid protein. J Biol Chem 2004; 279:34083 - 34086
   PubMed Web of Science ®Google Scholar
• Schafer A, Bogerd HP, Cullen BR. Specific packaging of APOBEC3G into HIV-1 virions is mediated by the nucleocapsid domain of the gag polyprotein precursor. Virology 2004; 328:163 - 168
   PubMed Web of Science ®Google Scholar
• Barbee SA, Estes PS, Cziko AM, Hillebrand J, Luedeman RA, Coller JM, et al. Staufen- and FMRP-containing neuronal RNPs are structurally and functionally related to somatic P bodies. Neuron 2006; 52:997 - 1009
   PubMed Web of Science ®Google Scholar
• Furtak V, Mulky A, Rawlings SA, Kozhaya L, Lee K, Kewalramani VN, et al. Perturbation of the P-body component Mov10 inhibits HIV-1 infectivity. PLoS One 2010; 5:9081
   PubMed Web of Science ®Google Scholar
• Gallois-Montbrun S, Kramer B, Swanson CM, Byers H, Lynham S, Ward M, et al. Antiviral protein APOBEC3G localizes to ribonucleoprotein complexes found in P bodies and stress granules. J Virol 2007; 81:2165 - 2178
   PubMed Web of Science ®Google Scholar
• Nathans R, Chu CY, Serquina AK, Lu CC, Cao H, Rana TM. Cellular microRNA and P bodies modulate host-HIV-1 interactions. Mol Cell 2009; 34:696 - 709
   PubMed Web of Science ®Google Scholar
• Chable-Bessia C, Meziane O, Latreille D, Triboulet R, Zamborlini A, Wagschal A, et al. Suppression of HIV-1 replication by microRNA effectors. Retrovirology 2009; 6:26
   Google Scholar
• Pettit SC, Moody MD, Wehbie RS, Kaplan AH, Nantermet PV, Klein CA, et al. The p2 domain of human immunodeficiency virus type 1 Gag regulates sequential proteolytic processing and is required to produce fully infectious virions. J Virol 1994; 68:8017 - 8027
   PubMed Web of Science ®Google Scholar
• Qualley DF, Stewart-Maynard KM, Wang F, Mitra M, Gorelick RJ, Rouzina I, et al. C-terminal domain modulates the nucleic acid chaperone activity of human T-cell leukemia virus type 1 nucleocapsid protein via an electrostatic mechanism. J Biol Chem 2010; 285:295 - 307
   PubMed Web of Science ®Google Scholar
• Stewart-Maynard KM, Cruceanu M, Wang F, Vo MN, Gorelick RJ, Williams MC, et al. Retroviral nucleocapsid proteins display nonequivalent levels of nucleic acid chaperone activity. J Virol 2008; 82:10129 - 10142
   PubMed Web of Science ®Google Scholar
• Cruceanu M, Urbaneja MA, Hixson CV, Johnson DG, Datta SA, Fivash MJ, et al. Nucleic acid binding and chaperone properties of HIV-1 Gag and nucleocapsid proteins. Nucleic Acids Res 2006; 34:593 - 605
   PubMed Web of Science ®Google Scholar
• Chapman KB, Bystrom AS, Boeke JD. Initiator methionine tRNA is essential for Ty1 transposition in yeast. Proc Natl Acad Sci USA 1992; 89:3236 - 3240
   PubMed Web of Science ®Google Scholar
• Keeney JB, Chapman KB, Lauermann V, Voytas DF, Astrom SU, von Pawel-Rammingen U, et al. Multiple molecular determinants for retrotransposition in a primer tRNA. Mol Cell Biol 1995; 15:217 - 226
   PubMedGoogle Scholar
• Ke N, Gao X, Keeney JB, Boeke JD, Voytas DF. The yeast retrotransposon Ty5 uses the anticodon stemloop of the initiator methionine tRNA as a primer for reverse transcription. RNA 1999; 5:929 - 938
   PubMed Web of Science ®Google Scholar
• Lin JH, Levin HL. A complex structure in the mRNA of Tf1 is recognized and cleaved to generate the primer of reverse transcription. Genes Dev 1997; 11:270 - 285
   PubMed Web of Science ®Google Scholar
• Cristofari G, Ficheux D, Darlix JL. The GAG-like protein of the yeast Ty1 retrotransposon contains a nucleic acid chaperone domain analogous to retroviral nucleocapsid proteins. J Biol Chem 2000; 275:19210 - 19217
   PubMed Web of Science ®Google Scholar
• Clark DJ, Bilanchone VW, Haywood LJ, Dildine SL, Sandmeyer SB. A yeast sigma composite element, TY3, has properties of a retrotransposon. J Biol Chem 1988; 263:1413 - 1423
   PubMed Web of Science ®Google Scholar
• Gabus C, Ficheux D, Rau M, Keith G, Sandmeyer S, Darlix JL. The yeast Ty3 retrotransposon contains a 5′-3′ bipartite primer-binding site and encodes nucleocapsid protein NCp9 functionally homologous to HIV-1 NCp7. EMBO J 1998; 17:4873 - 4880
   PubMed Web of Science ®Google Scholar
• Cristofari G, Gabus C, Ficheux D, Bona M, Le Grice SF, Darlix JL. Characterization of active reverse transcriptase and nucleoprotein complexes of the yeast retrotransposon Ty3 in vitro. J Biol Chem 1999; 274:36643 - 36648
   PubMed Web of Science ®Google Scholar
• Friant S, Heyman T, Bystrom AS, Wilhelm M, Wilhelm FX. Interactions between Ty1 retrotransposon RNA and the T and D regions of the tRNA(iMet) primer are required for initiation of reverse transcription in vivo. Mol Cell Biol 1998; 18:799 - 806
   PubMed Web of Science ®Google Scholar
• Friant S, Heyman T, Wilhelm ML, Wilhelm FX. Extended interactions between the primer tRNAi(Met) and genomic RNA of the yeast Ty1 retrotransposon. Nucleic Acids Res 1996; 24:441 - 449
   PubMedGoogle Scholar
• Cristofari G, Bampi C, Wilhelm M, Wilhelm FX, Darlix JL. A 5′-3′ long-range interaction in Ty1 RNA controls its reverse transcription and retrotransposition. EMBO J 2002; 21:4368 - 4379
   PubMed Web of Science ®Google Scholar
• Ooms M, Abbink TE, Pham C, Berkhout B. Circularization of the HIV-1 RNA genome. Nucleic Acids Res 2007; 35:5253 - 5261
   PubMed Web of Science ®Google Scholar
• Piekna-Przybylska D, DiChiacchio L, Mathews DH, Bambara RA. A sequence similar to tRNA 3 Lys gene is embedded in HIV-1 U3-R and promotes minus-strand transfer. Nat Struct Mol Biol 2010; 17:83 - 89
   PubMed Web of Science ®Google Scholar
• Song M, Balakrishnan M, Gorelick RJ, Bambara RA. A succession of mechanisms stimulate efficient reconstituted HIV-1 minus strand strong stop DNA transfer. Biochemistry 2009; 48:1810 - 1819
   PubMed Web of Science ®Google Scholar
• Chapman KB, Boeke JD. Isolation and characterization of the gene encoding yeast debranching enzyme. Cell 1991; 65:483 - 492
   PubMed Web of Science ®Google Scholar
• Bushman FD, Malani N, Fernandes J, D'Orso I, Cagney G, Diamond TL, et al. Host cell factors in HIV replication: meta-analysis of genome-wide studies. PLoS Pathog 2009; 5:1000437
   PubMed Web of Science ®Google Scholar
• Cheng Z, Menees TM. RNA branching and debranching in the yeast retrovirus-like element Ty1. Science 2004; 303:240 - 243
   PubMed Web of Science ®Google Scholar
• Ye Y, De Leon J, Yokoyama N, Naidu Y, Camerini D. DBR1 siRNA inhibition of HIV-1 replication. Retrovirology 2005; 2:63
   PubMed Web of Science ®Google Scholar
• Coombes CE, Boeke JD. An evaluation of detection methods for large lariat RNAs. RNA 2005; 11:323 - 331
   PubMed Web of Science ®Google Scholar
• Watts JM, Dang KK, Gorelick RJ, Leonard CW, Bess JW Jr, Swanstrom R, et al. Architecture and secondary structure of an entire HIV-1 RNA genome. Nature 2009; 460:711 - 716
   PubMed Web of Science ®Google Scholar