52
Views
20
CrossRef citations to date
0
Altmetric
Original Article

A Notable Example of an Evolutionary Conserved Gene: Studies on a Putative DNA Helicase TIP49

, , &
Pages 37-42 | Received 17 Jun 1998, Published online: 11 Jul 2009

References

  • Allison L. A., Moyle M., Shales M., Ingles C. J. Extensive homology among the largest subunits of eukaryotic and prokaryotic RNA polymerases. Cell 1985; 42: 599–610
  • Confalonieri F., Duguet M. A 200-amino acid ATPase module in search of a basic function. Bioessays 1995; 17: 639–650
  • Goffeau A., Aert R. The yeast genome directory. Nature 1997; 387: 1–105, suppl.
  • Gorbalenya A. E., Koonin E. V. Helicases: amino acid sequence comparisons and structure-function relationships. Curr. Opin. Struct. Biol 1993; 3: 419–429
  • Horikoshi M., Wang C. K., Fujü H., Cromlish J. A., Weil P. A., Roeder R. G. Cloning and structure of a yeast gene encoding a general transcription initiation factor TFIID that binds to the TATA box. Nature 1989; 341: 299–303
  • Iwasaki H., Takahagi M., Nakata A., Shinagawa H. Escherichia coli RuvA and RuvB proteins specifically interact with Holliday junctions and promote branch migration. Genes Dev. 1992; 6: 2214–2220
  • Kanemaki M., Makino Y., Yoshida T., Kishimoto T., Koga A., Yamamoto K., Yamamoto M., Moncollin V., Egly J.-M., Muramatsu M., Tamura T. Molecular Cloning of a Rat 49-kDa TBP-interacting protein (TIP49) that is highly homologous to the bacterial RuvB. Biochem. Biophys. Res. Commun. 1997; 235: 64–68
  • Klenk H.-P., Clayton R. A. The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus. Nature 1997; 390: 364–370
  • Makino Y., Mimori T., Koike C., Kanemaki M., Kurokawa Y., Inoue S., Kishimoto T., Tamura T. TIP49, homologous to the bacterial DNA helicase RuvB, acts as an autoantigen in human. Biochem. Biophys. Res. Commun. 1998; 245: 819–823
  • Shinagawa H., Makino K., Amemura M., Kimura S., Iwasaki H., Nakata A. Structure and regulation of the Escherichia coli ruv operon involved in DNA repair and recombination. J. Bacterial 1988; 170: 4322–4329
  • Shinohara A., Ogawa H., Matsuda Y., Ushio N., Ikeo K., Ogawa T. Cloning of human, mouse and fission yeast recombination genes homologous to RAD51 and recA. Nature genetics 1993; 4: 239–243
  • Svejstrup J. Q., Vichi P., Egly J.-M. The multiple roles of transcription/repair factor TFIIH. Trends Biochem. Sci. 1996; 21: 346–350
  • Thompson J. D., Higgins D. G., Gibson T. J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res. 1994; 22: 4673–4680
  • Tong J., Wetmur J. G. Cloning, sequencing, and expression of ruvB and characterization of RuvB proteins from two distantly related thermophilic eubacteria. J. Bacterial. 1996; 178: 2695–2700
  • Tsaneva I. R., Muller B., West S. C. RuvA and RuvB proteins of Escherichia coii exhibit DNA helicase activity in vitro. Proc. Natl. Acad. Sci. USA 1993; 90: 1315–1319
  • Walker J. E., Saraste M., Runswick M. J., Gay N. J. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotides binding fold. EMBO J. 1982; 1: 945–951
  • Wong S. W., Wahl A. F., Yuan P.-M., Arai N., Pearson B. E., Arai K., Korn D., Hunkapiller M. W., Wang T.-F. S. Human DNA polymerase α gene expression is cell proliferation dependent and its primary structure is similar to both prokaryotic replicative DNA polymerases. EMBO J. 1988; 7: 37–47

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.