25
Views
30
CrossRef citations to date
0
Altmetric
Transcriptional Regulation

The Rpb6 Subunit of Fission Yeast RNA Polymerase II Is a Contact Target of the Transcription Elongation Factor TFIIS

, , , &
Pages 1263-1270 | Received 05 Aug 1999, Accepted 16 Nov 1999, Published online: 28 Mar 2023

REFERENCES

  • Agarwal, K., Baek, K., Jeon, C., Miyamoto, K., Ueno, A., and Yoon, H.. 1991. Stimulation of transcript elongation requires both the zinc finger and RNA polymerase II binding domains of human TFIIS. Biochemistry 30:7842–7851
  • Ahn, B.-Y., Gershon, P. D., Jones, E. V., and Moss, R.. 1990. Identification of rpo30, a vaccinia virus RNA polymerase gene with structural similarity to a eucaryotic transcription elongation factor. Mol. Cell. Biol. 10:5433–5441
  • Alfa, C., Fantes, P., Hyams, J., McLeod, M., and Warbrick, E.. 1993. Experiments with fission yeast: a laboratory course manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y
  • Archambault, J., Lacroute, F., Ruet, A., and Friesen, J. D.. 1992. Genetic interaction between transcription elongation factor TFIIS and RNA polymerase II. Mol. Cell. Biol. 12:4142–4152
  • Archambault, J., Schappert, K. T., and Friesen, J. D.. 1990. A suppressor of an RNA polymerase II mutation of Saccharomyces cerevisiae encodes a subunit common to RNA polymerases I, II, and III. Mol. Cell. Biol. 10:6123–6131
  • Awrey, D. E., Weilbaecher, R. G., Hemming, S. A., Orlicky, S. M., Kane, C. M., and Edwards, A. M.. 1997. Transcription elongation through DNA arrest site. J. Biol. Chem. 272:14747–14754
  • Awrey, D. E., Shimasaki, N., Koth, C., Weilbaecher, R., Olmsted, V., Kazanis, S., Shan, X., Arellano, J., Arrowsmith, C. H., Kane, C. M., and Edwards, A. M.. 1998. Yeast transcript elongation factor (TFIIS), structure and function. J. Biol. Chem. 273:22595–22605
  • Azuma, Y., Yamagishi, M., Ueshima, R., and Ishihama, A.. 1993. Subunits of the Schizosaccharomyces pombe RNA polymerase II: enzyme purification and structure of the subunit 3 gene. Nucleic Acids Res. 21:3749–3754
  • Beant, B., Huet, J., Sentenac, A., and Fromageot, P.. 1983. Analysis of yeast RNA polymerases with subunit-specific antibodies. J. Biol. Chem. 258:11968–11973
  • Dixon, L. K., Twigg, S. R. K., Baylis, S. A., Vydelingum, S., Bristow, C., Hammond, J. M., and Smit, G. L.. 1994. Nucleotide sequence of a 55 kbp region from the right end of the genome of a pathogenic African swine fever virus isolate. J. Gen. Virol. 75:1655–1684
  • Exinger, F., and Lacroute, F.. 1992. 6-Azauracil inhibition of GTP biosynthesis in Saccharomyces cerevisiae. Curr. Genet. 22:9–11
  • Fromant, M., Blanquet, S., and Plateau, P.. 1995. Direct random mutagenesis of gene-sized DNA fragments using polyphosphate chain reaction. Arch. Biochem. 224:347–353
  • Grimm, C., and Kohli, J.. 1988. Observations on integrative transformation in Saccharomyces pombe. Mol. Gen. Genet. 215:87–93
  • Ishiguro, A., Kimura, M., Yasui, K., Iwata, A., Ueda, S., and Ishihama, A.. 1998. Two large subunits of the fission yeast RNA polymerase II provide platforms for the assembly of small subunits. J. Mol. Biol. 279:703–712
  • Ishiguro, J., and Kobayashi, W.. 1995. A practical method for fission yeast transformation by electroporation. Jpn. J. Genet. 70:1–6
  • Ishihama, A.. 1981. Subunit assembly of Escherichia coli RNA polymerase. Adv. Biophys. 14:1–35
  • Ishihama, A., Kimura, M., and Mitsuzawa, H.. 1998. Subunits of yeast RNA polymerases in structure and function. Curr. Opin. Microbiol. 1:190–196
  • Izban, M. G., and Luse, D. S.. 1992. The RNA polymerase II ternary complex cleaves the nascent transcript in a 3′-5′ direction in the presence of elongation factor SII. Genes Dev. 6:1342–1356
  • Kimura, M., Ishiguro, A., and Ishihama, A.. 1997. RNA polymerase II subunits 2, 3 and 11 form a core subassembly with DNA binding activity. J. Biol. Chem. 272:25851–25855
  • Langer, D., Hain, J., Thuriaux, P., and Zillig, W.. 1995. Transcription in archaea: similarity to that in eucarya. Proc. Natl. Acad. Sci. USA 92:5768–5772
  • Lanzendörfer, M., Smid, A., Klinger, C., Schults, P., Sentenac, A., Carles, C., and Riva, M.. 1997. A shared subunit belongs to the eukaryotic core RNA polymerase. Genes Dev. 11:1037–1047
  • Lennon, J. C.III, Wind, M., Saunders, L., Hock, M. B., and Reins, D.. 1998. Mutations in RNA polymerase II and elongation factor IIS severely reduce mRNA levels in Saccharomyces cerevisiae. Mol. Cell. Biol. 18:5771–5779
  • Lu, Z., Kutish, G. F., Sussman, M. D., and Rock, D. L.. 1993. An African swine fever virus gene with a similarity to eukaryotic RNA polymerase subunit 6. Nucleic Acids Res. 21: 2940
  • Maundrell, K.. 1990. nmt1 of fission yeast. J. Biol. Chem. 265:10857–10864
  • McKune, K., and Woychik, N. A.. 1994. Functional substitution of an essential yeast RNA polymerase subunit by a highly conserved mammalian counterpart. Mol. Cell. Biol. 14:4155–4159
  • Miyao, T., Honda, A., Qu, Z., and Ishihama, A.. 1998. Mapping of Rpb3 and Rpb5 contact sites on two large subunits, Rpb1 and Rpb2, of the fission yeast RNA polymerase II. Mol. Gen. Genet. 259:123–129
  • Nakanishi, T., Nakano, A., Nomura, K., Sekimizu, K., and Natori, S.. 1995. Structure-function relationship of yeast SII in terms of stimulation of RNA polymerase II, arrest relief, and suppression of 6-azauracil sensitivity. J. Biol. Chem. 270:8991–8997
  • Nouraini, S., Archambault, J., and Friesen, J. D.. 1996. Rpo26p, a subunit common to yeast RNA polymerases, is essential for the assembly of RNA polymerases I and II and for stability of the largest subunits of these enzymes. Mol. Cell. Biol. 16:5985–5996
  • Olmsted, V. K., Awrey, D. E., Koth, C., Shan, X., Morin, P. E., Kazanis, S., Edwards, A. M., and Arrowsmith, C. H.. 1998. Yeast transcript elongation factor (TFIIS), structure and function. J. Biol. Chem. 273:22589–22594
  • Powell, W., and Reines, D.. 1996. Mutations in the second largest subunit of RNA polymerase II cause 6-azauracil sensitivity in yeast and increased transcriptional arrest in vitro. J. Biol. Chem. 271:6866–6873
  • Reines, D., Chamberlin, M. J., and Kane, C. K.. 1989. Transcription elongation factor SII (TFIIS) enables RNA polymerase II to elongate through a block to transcription in a human gene in vitro. J. Biol. Chem. 264:10799–10809
  • Reines, D.. 1992. Elongation factor-dependent transcript shortening by template-engaged RNA polymerase II. J. Biol. Chem. 267:3795–3800
  • Rodrigez, J. M., Salas, M. L., and Viñuela, E.. 1992. Genes homologous to ubiquitin-conjugating proteins and eukaryotic transcription factor SII in African swine fever virus. Virology 186:40–52
  • Sakurai, H., and Ishihama, A.. 1997. Gene organization and protein sequence of the small subunits of Schizosaccharomyces pombe RNA polymerase II. Gene 196:165–174
  • Sakurai, H., Mitsuzawa, H., Kimura, M., and Ishihama, A.. 1999. Rpb4 subunit of the fission yeast Schizosaccharomyces pombe RNA polymerase II is essential for cell viability and similar in structure to the corresponding subunits of higher eukaryotes. Mol. Cell. Biol. 19:7511–7518
  • Sawadogo, M., Huet, J., and Fromageot, P.. 1980. Similar binding site for P37 factor on yeast RNA polymerases A and B. Biochem. Biophys. Res. Commun. 96:258–264
  • Sawadogo, M., Sentenac, A., and Fromageot, P.. 1980. Interaction of a new polypeptide with yeast RNA polymerase B. J. Biol. Chem. 255:12–15
  • Sekimizu, K., Nakanishi, Y., Mizuno, D., and Natori, S.. 1989. Purification and preparation of antibody to RNA polymerase II stimulatory factors from Ehrlich ascites tumor cells. Biochemistry 18:1582–1587
  • Shimoaraiso, M., Nakanishi, T., Kubo, T., and Natori, S.. 1997. Identification of the region in yeast S-II that defines species specificity in its interaction with RNA polymerase II. J. Biol. Chem. 272:26550–26554
  • Shpakovski, G. V.. 1994. The fission yeast Schizosaccharomyces pombe rpb6 gene encodes the common phosphorylated subunit of RNA polymerase and complements a mutation in the corresponding gene of Saccharomyces cerevisiae. Gene 147:67–69
  • Shpakovski, G. V., Acker, I., Wintzerith, M., Lacroix, J.-F., Thuriaux, P., and Vigneron, M.. 1995. Four subunits that are shared by the three classes of RNA polymerase are functionally interchangeable between Homo sapiens and Saccharomyces cerevisiae. Mol. Cell. Biol. 15:4702–4710
  • Sopta, M., Carthew, R. W., and Greenblatt, L.. 1985. Isolation of three proteins that bind to mammalian RNA polymerase II. J. Biol. Chem. 260:10353–10360
  • Svetlov, V., and Cooper, T. G.. 1998. Efficient PCR-based random mutagenesis of subgenic (100 bp) DNA fragments. Yeast 14:89–91
  • Thuriaux, P., and Sentenac, A.. Yeast nuclear RNA polymerases p. 1–48. In Broach, J. R., Pringle, J. R., and Jones, E. W. The molecular and cellular biology of the yeast Saccharomyces, vol. II. Gene expression. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y
  • Williams, A. A., and Kane, C. M.. 1996. 1992. Isolation and characterization of the Schizosaccharomyces pombe gene encoding transcript elongation factor TFIIS. Yeast 12:227–236
  • Woychik, N. A., Liao, S., Kolodziej, P. A., and Young, R. A.. 1990. Subunits shared by eukaryotic nuclear RNA polymerases. Genes Dev. 4:313–323
  • Woychik, N. A., and Young, R. A.. 1994. Exploring RNA polymerase II structure and function Transcription: mechanisms and regulation. Conaway, R. C., and Conaway, J. W. 227–242 Raven Press, New York, N.Y
  • Wu, J., Awrey, D. E., Edwards, A. M., Archambault, J., and Friesen, J. D.. 1996. In vitro characterization of mutant yeast RNA polymerase II with reduced binding for elongation factor TFIIS. Proc. Natl. Acad. Sci. USA 93:11552–11557
  • Yasui, K., Ishiguro, A., and Ishihama, A.. 1998. Location of subunit-subunit contact sites on RNA polymerase II from the fission yeast Schizosaccharomyces pombe. Biochemistry 37:5542–5548
  • Zou, C., Fujita, N., Igarashi, K., and Ishihama, A.. 1992. Mapping the Escherichia coli RNA polymerase contact site I for cAMP receptor protein. Mol. Microbiol. 6:2599–2605

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.