Synthesis and Characterization of the Spore Proteins of Bacillus subtilis YdhD, YkuD, and YkvP, Which Carry a Motif Conserved among Cell Wall Binding Proteins

2000 ◽  
Vol 128 (4) ◽  
pp. 655-663 ◽  
Author(s):  
T. Kodama ◽  
H. Takamatsu ◽  
K. Asai ◽  
N. Ogasawara ◽  
Y. Sadaie ◽  
...  
Keyword(s):  
Cell Wall ◽  
Bacillus Subtilis ◽  
Binding Proteins ◽  
Synthesis And Characterization ◽  
Cell Wall Binding ◽  
Spore Proteins

scholarly journals Characterization of TseB: A new actor in cell wall elongation in Bacillus subtilis

2021 ◽  
Author(s):  
Jordan Delisle ◽  
Baptiste Cordier ◽  
Stéphane Audebert ◽  
Matthieu Pophillat ◽  
Caroline Cluzel ◽  
...  
Keyword(s):  
Cell Wall ◽  
Bacillus Subtilis

scholarly journals Characterization of a Bacillus subtilis Thermosensitive Teichoic Acid-Deficient Mutant: Gene mnaA (yvyH) Encodes the UDP-N-Acetylglucosamine 2-Epimerase

2002 ◽  
Vol 184 (15) ◽  
pp. 4316-4320 ◽  
Author(s):  
Blazenka Soldo ◽  
Vladimir Lazarevic ◽  
Harold M. Pooley ◽  
Dimitri Karamata
Keyword(s):  
Cell Wall ◽  
Bacillus Subtilis ◽  
Cell Morphology ◽  
Teichoic Acid ◽  
Mutant Gene ◽  
Deficient Mutant ◽  
Phosphate Content ◽  
Nonpermissive Temperature ◽  
Coccoid Cell

ABSTRACT The Bacillus subtilis thermosensitive mutant ts-21 bears two C-G→T-A transitions in the mnaA gene. At the nonpermissive temperature it is characterized by coccoid cell morphology and reduced cell wall phosphate content. MnaA converts UDP-N-acetylglucosamine into UDP-N-acetylmannosamine, a precursor of the teichoic acid linkage unit.

scholarly journals Rod Shape Determination by the Bacillus subtilis Class B Penicillin-Binding Proteins Encoded by pbpA and pbpH

2003 ◽  
Vol 185 (16) ◽  
pp. 4717-4726 ◽  
Author(s):  
Yuping Wei ◽  
Teresa Havasy ◽  
Derrell C. McPherson ◽  
David L. Popham
Keyword(s):  
Cell Wall ◽  
Bacillus Subtilis ◽  
Binding Proteins ◽  
Structural Integrity ◽  
Sequence Similarity ◽  
Inducible Promoter ◽  
Penicillin Binding Proteins ◽  
Peptidoglycan Cell Wall ◽  
Class B ◽  
Shape Determination

ABSTRACT The peptidoglycan cell wall determines the shape and structural integrity of a bacterial cell. Class B penicillin-binding proteins (PBPs) carry a transpeptidase activity that cross-links peptidoglycan strands via their peptide side chains, and some of these proteins are directly involved in cell shape determination. No Bacillus subtilis PBP with a clear role in rod shape maintenance has been identified. However, previous studies showed that during outgrowth of pbpA mutant spores, the cells grew in an ovoid shape for several hours before they recovered and took on a normal rod shape. It was postulated that another PBP, expressed later during outgrowth, was able to compensate for the lack of the pbpA product, PBP2a, and to guide the formation of a rod shape. The B. subtilis pbpH (ykuA) gene product is predicted to be a class B PBP with greatest sequence similarity to PBP2a. We found that a pbpH-lacZ fusion was expressed at very low levels in early log phase and increased in late log phase. A pbpH null mutant was indistinguishable from the wild-type, but a pbpA pbpH double mutant was nonviable. When pbpH was placed under the control of an inducible promoter in a pbpA mutant, viability was dependent on pbpH expression. Growth of this strain in the absence of inducer resulted in conversion of the cells from rods to ovoid/round shapes and lysis. We conclude that PBP2a and PbpH play redundant roles in formation of a rod-shaped peptidoglycan cell wall.

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