The life-cycle proteins RodA of Escherichia coli and SpoVE of Bacillus subtilis have very similar primary structures - PubMed (original) (raw)

Comparative Study

The life-cycle proteins RodA of Escherichia coli and SpoVE of Bacillus subtilis have very similar primary structures

B Joris et al. Mol Microbiol. 1990 Mar.

Free article

Abstract

Comparison of the predicted amino acid sequence of the cell-cycle RodA protein with the National Research Foundation protein sequence database shows that the 370-amino-acid RodA, a protein that is essential for wall elongation in Escherichia coli and maintenance of the rod shape of the cell, is highly analogous, in terms of primary structure, with the Bacillus subtilis SpoVE protein involved in stage V of sporulation.

PubMed Disclaimer

Similar articles

• Structural similarity among Escherichia coli FtsW and RodA proteins and Bacillus subtilis SpoVE protein, which function in cell division, cell elongation, and spore formation, respectively.
  Ikeda M, Sato T, Wachi M, Jung HK, Ishino F, Kobayashi Y, Matsuhashi M. Ikeda M, et al. J Bacteriol. 1989 Nov;171(11):6375-8. doi: 10.1128/jb.171.11.6375-6378.1989. J Bacteriol. 1989. PMID: 2509435 Free PMC article.
• A Bacillus subtilis morphogene cluster that includes spoVE is homologous to the mra region of Escherichia coli.
  Henriques AO, de Lencastre H, Piggot PJ. Henriques AO, et al. Biochimie. 1992 Jul-Aug;74(7-8):735-48. doi: 10.1016/0300-9084(92)90146-6. Biochimie. 1992. PMID: 1391053
• Control of cell shape and elongation by the rodA gene in Bacillus subtilis.
  Henriques AO, Glaser P, Piggot PJ, Moran CP Jr. Henriques AO, et al. Mol Microbiol. 1998 Apr;28(2):235-47. doi: 10.1046/j.1365-2958.1998.00766.x. Mol Microbiol. 1998. PMID: 9622350
• Taking shape: control of bacterial cell wall biosynthesis.
  Stewart GC. Stewart GC. Mol Microbiol. 2005 Sep;57(5):1177-81. doi: 10.1111/j.1365-2958.2005.04760.x. Mol Microbiol. 2005. PMID: 16101993 Review.
• Tus and the terminators: the arrest of replication in prokaryotes.
  Kuempel PL, Pelletier AJ, Hill TM. Kuempel PL, et al. Cell. 1989 Nov 17;59(4):581-3. doi: 10.1016/0092-8674(89)90001-9. Cell. 1989. PMID: 2510933 Review. No abstract available.

Cited by

• The Escherichia coli cell division protein FtsW is required to recruit its cognate transpeptidase, FtsI (PBP3), to the division site.
  Mercer KL, Weiss DS. Mercer KL, et al. J Bacteriol. 2002 Feb;184(4):904-12. doi: 10.1128/jb.184.4.904-912.2002. J Bacteriol. 2002. PMID: 11807049 Free PMC article.
• The sigma factors of Bacillus subtilis.
  Haldenwang WG. Haldenwang WG. Microbiol Rev. 1995 Mar;59(1):1-30. doi: 10.1128/mr.59.1.1-30.1995. Microbiol Rev. 1995. PMID: 7708009 Free PMC article. Review.
• The Enterococcus hirae R40 penicillin-binding protein 5 and the methicillin-resistant Staphylococcus aureus penicillin-binding protein 2' are similar.
  el Kharroubi A, Jacques P, Piras G, Van Beeumen J, Coyette J, Ghuysen JM. el Kharroubi A, et al. Biochem J. 1991 Dec 1;280 ( Pt 2)(Pt 2):463-9. Biochem J. 1991. PMID: 1747121 Free PMC article.
• Functional analysis of the cell division protein FtsW of Escherichia coli.
  Pastoret S, Fraipont C, den Blaauwen T, Wolf B, Aarsman ME, Piette A, Thomas A, Brasseur R, Nguyen-Distèche M. Pastoret S, et al. J Bacteriol. 2004 Dec;186(24):8370-9. doi: 10.1128/JB.186.24.8370-8379.2004. J Bacteriol. 2004. PMID: 15576787 Free PMC article.
• Determinants for the subcellular localization and function of a nonessential SEDS protein.
  Real G, Fay A, Eldar A, Pinto SM, Henriques AO, Dworkin J. Real G, et al. J Bacteriol. 2008 Jan;190(1):363-76. doi: 10.1128/JB.01482-07. Epub 2007 Nov 2. J Bacteriol. 2008. PMID: 17981970 Free PMC article.

Publication types

MeSH terms

Substances

LinkOut - more resources

• Full Text Sources

  • ORBi (University of Liege)
  • Wiley