The Life-Cycle Proteins Roda of Escherichia Coli and Spove of Bacillus Subtilis Have Very Similar Primary Structures

Proteins; Morphology; Sporulation; Aminoacid sequence; Sequence alignment; Homology; Escherichia coli; Bacillus subtilis; Escherichieae; Enterobacteriaceae; Bacteria; Bacillaceae; Bacillales; Protéine; Morphologie; Séquence aminoacide; Alignement séquence; Homologie; Protéine RodA; Protéine SpoVE; Bactérie; Proteina; Morfología; Esporulación; Secuencia aminoácido; Alineación secuencia; Homologia

Abstract :

[en] 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.

Disciplines :

Biochemistry, biophysics & molecular biology

Author, co-author :

Joris, Bernard ; Université de Liège - ULiège > Institut de Chimie > Service de Microbiologie

Dive, Georges ; Université de Liège - ULiège > Institut de Chimie > Service de Microbiologie

Henriques, A.; Instituto Gulbenkian de Cienca > Laboratorio de Genetica Molecular

Piggot, P. J.; Temple University School of Medecine > Departement of Microbiology and Immunology

Ghuysen, Jean-Marie ; Université de Liège - ULiège > Institut de Chimie > Service de Microbiologie

Language :

English

Title :

The Life-Cycle Proteins Roda of Escherichia Coli and Spove of Bacillus Subtilis Have Very Similar Primary Structures

Publication date :

March 1990

Journal title :

Molecular Microbiology

ISSN :

0950-382X

eISSN :

1365-2958

Publisher :

Blackwell Publishing, Oxford, United Kingdom

Volume :

Issue :

Pages :

513-517

Peer reviewed :

Peer Reviewed verified by ORBi

Funders :

F.R.S.-FNRS - Fonds de la Recherche Scientifique

Available on ORBi :

since 30 December 2009

Statistics

Number of views

161 (2 by ULiège)

Number of downloads

160 (0 by ULiège)

More statistics

Scopus citations^®

Scopus citations^®
without self-citations

OpenCitations

OpenAlex citations

Bibliography

Adachi H., Ohta T., Matsuzawa H. (1987) A water‐soluble form of penicillin‐binding protein 2 of Escherichia coli construction by site‐directed mutagenesis. FEBS Lett 226:150-154.
Asoh S., Matsuzawa H., Ishino F., Strominger J., Matsuhashi M., Ohta T. (1986) Nucleotide sequence of the pbpA gene and characteristics of the deduced amino acid sequence of penicillin‐binding protein 2 of Escherichia coli K12. Eur J Biochem 160:231-238.
Bartholomé‐De Belder J., Nguyen‐Disteche M., Houba‐Herin N., Ghuysen J.M., Maruyama I.N., Hara H., Hirota Y., Inouye M. (1988) Overexpression, solubilization and refolding of a genetically engineered derivative of the penicillin‐binding protein 3 of Escherichia coli K12. Mol Microbiol 2:519-525.
Beall B., Lowe M., Lutkenhaus J. (1988) Cloning and characterization of Bacillus subtilis homologs of Escherichia coli cell division genes ftsZ and ftsA. J Bacteriol 170:4855-4864.
Begg K.J., Spratt B.G., Donachle W.D. Interaction between membrane proteins PBP3 and RodA is required for normal cell shape and division in Escherichia coli J Bacteriol 1986, 167:1004-1008.
Bouloc P., Jaffé A., D'Ari R. (1989) The Escherichia coli lov gene product connects peptidoglycan synthesis, ribosomes and growth rate. EMBO J 8:317-323.
Bowler D.L., Spratt B.G. (1989) Membrane topology of penicillin‐binding protein 3 of Escherichia coli. Mol Microbiol 3:1277-1286.
Broome‐Smith J.K., Loannidis I., Edelman A., Spratt B.G. (1988) Nucleotide sequences of the penicillin‐binding protein 5 and 6 genes of Escherichia coli. Nucleic Acids Research 16:1617.
Buchanan C.E., Neyman S.L. (1986) Correlation of penicillin‐binding protein composition with different functions of two membranes in Bacillus subtilis forespores. J Bacteriol 165:498-503.
Buchanan C.E., Sowell M.O. (1983) Stability and synthesis of the penicillin‐binding proteins during sporulation. J Bacteriol 156:545-551.
Bugaichuk U.D. (1987) Studies of transcriptional regulation of the Bacillus subtilis developmental gene spoVE. J Gen Microbiol 133:2349-2357.
Bugaichuk U.D., Piggot P.J. (1986) Nucleotide sequence of the Bacillus subtilis developmental gene spoVE. J Gen Microbiol 132:1883-1890.
Coote J.G. (1972) Sporulation of Bacillus subtilis. Characterization of oligosporagenous mutants and comparison of their phenotype with those of asporogenous mutants. J Gen Microbiol 71:1-15.
Devereux J., Haeberli P., Smithies O. (1984) A comprehensive set of sequence analysis programs for the VAX. Nucl Acids Res 12:387-395.
Donachie W.D., Begg K.J., Lutkenhaus J.F., Salmond G.P.C., Martinez‐Salas E., Vicente M. (1979) Role of the ftsA gene product In control of Escherichia coli cell division. J Bacteriol 140:388-394.
Engelman D.M., Steitz T.A., Goldman A. (1986) Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins. Annu Rev Biochem Biophys Chem 15:321-353.
Goad W.B., Kanehisa M.T. (1982) Pattern recognition in nucleic acid sequences. I. A general method for finding local homologies and symmetries. Nucl Acids Res 10:247-263.
Ishino F., Park W., Tomiako S., Tamaki S., Takase I., Kunugita K., Matsuzawa H., Asoh S., Ohta T., Spratt B.G., Matsuhashi M. (1986) Peptidoglycan synthetic activities in membranes of Escherichia coli caused by overproduction of penicillin‐binding protein 2 and RodA protein. J Biol Chem 261:7024-7031.
Jones C.A., Holland I.B. (1985) Role of the SfiB (FtsZ) protein in division inhibition during the SOS response in E. coli: FtsZ stabilizes the inhibitor SfiA in maxicells. Proc Natl Acad Sci USA 82:6045-6049.
Kyte J., Doolittle R.F. (1982) A simple method for displaying the hydropathic character of a protein. J Mol Biol 157:105-132.
Matsuzawa H., Asoh S., Kunai K., Muraiso K., Takasuga A., Ohta T. (1989) Nucleotide sequence of the rodA gene, responsible for the rod shape of Escherichia coli: rodA. and the pbpA gene, encoding penicillin‐binding protein 2, constitute the rodA operon. J Bacteriol 171:558-560.
Nakamura M., Maruyama I.N., Soma M., Kato J., Suzuki H., Hirota Y. (1983) On the process of cellular division in Escherichia coli: nucleotide sequence of the gene for penicillin‐binding protein 3. Mol Gen Genet 191:1-9.
Ogura T., Bouloc P., Niki H., D'Ari R., Hiraga S., Jaffé A. (1989) Penicillin‐binding protein 2 is essential in wild‐type Escherichia coli but not in lov or cya mutants. J Bacteriol 171:3025-3030.
Piggot J.J., Coote J.G. (1976) Genetic aspects of bacterial endospore formation. Bacteriol Rev 40:908-962.
Pratt J.M., Jackson M.E., Holland I.B. (1986) The C terminus of penicillin‐binding protein 5 is essential for localisation of the E. coli inner membrane. EMBO J 5:2399-2405.
Robinson A.C., Kenan D.J., Hatfull G.F., Sullivan N.F., Spiegel‐berg R., Donachie W.D. (1984) DNA sequence and transcriptional organization of essential cell division genes ftsQ and ftsA of Escherichia coli: evidence for overlapping transcriptional units. J Bacteriol 160:546-555.
Robinson A.C., Collins J.F., Donachie W.D. (1987) Pro‐karyotic and eukaryotic cell‐cycle proteins. Nature 328:766.
Robinson A.C., Begg K.J., Sweeney J., Condie A., Donachie W.D. (1988) Mapping and characterization of mutants of the Escherichia coli cell division gene ftsA. Mol Microbiol 2:581-588.
Smith J.F., Waterman M.S. (1981) Comparison of bio‐sequences. Adv Appl Math 2:482-489.
Sowell M.O., Buchanan C.E. (1983) Changes in penicillin‐binding proteins during sporulation of Bacillus subtilis. J Bacteriol 153:1331-1337.
Stoker N.G., Broome‐Smith J.K., Edelman A., Spratt B.G. (1983) Organization and subcloning of the dacA‐rodA‐pbpA cluster of cell shape genes in Escherichia coli. J Bacteriol 155:847-853.
Stoker N.G., Pratt J.M., Spratt B.G. (1983) Identification of the fodA gene product of Escherichia coli. J Bacteriol 155:854-859.
Taschner P.E.M., Huls P.G., Pas E., Woidringh C.L. (1988) Division behavior and shape changes in isogenic ftsZ. ffsQ, ftsA, pbpB, and ffsE cell division mutants of Escherichia coli during temperature shift experiments. J Bacteriol 170:1533-1540.
Tinoco I., Borer P., Dengler B., Levine M., Uhlenbeck O., Crothers D., Gralta J. (1973) Improved estimation of secondary structure in ribonucleic acids. Nature New Biol 246:40-41.
Todd J.A., Bone E.J., Piggot P.J., Ellar D.J. (1983) Differential expression of penicillin‐binding protein structural genes during Bacillus subtilis sporulation. FEMS Microbiol Lett 18:197-202.
Todd J.A., Bone E.J., Ellar D.J. (1985) The sporutation‐specific penicillin‐binding protein 5a from Bacillus subtilis is a DD‐carboxypeptidase in vitro. Biochem J 230:825-828.
Tormo A., Vicente M. (1984) The ftsA gene product participates in formation of the Escherichia coli septum structure. J Bacteriol 157:779-784.
Tormo A., Ayala J.A., de Pedro M.A., Aldea M., Vicente M. (1986) Interaction of FtsA and PBP3 proteins in the Escherichia coli septum. J Bacteriol 166:985-992.
Tormo A., Martinez‐Sala E., Vicente M. (1980) Involvement of the ftsA gene product in late stages of the Escherichia coli cell cycle. J Bacteriol 141:806-813.
Uratani B., Lopez J.M., Freese E. (1983) Effect of decoyinine on peptidoglycan synthesis and turnover in Bacillus subtilis. J Bacteriol 154:261-268.
Ward J.E., Lutkenhaus J.F. (1985) Overproduction of FtsZ induces minicells in E coli. Cell 42:941-949.
Wilbur W.J., Lipman D.J. (1983) Rapid similarity searches of nucleic acid and protein data bank. Proc Natl Acad Sci USA 80:726-730.
Yi Q.M., Lutkenhaus J.F. (1985) The nucleotide sequence of the essential cell division gene ftsZ. Gene 36:241-247.