TY - JOUR
T1 - A cell wall protein (YqgA) is genetically related to the cell wall-degrading DL-endopeptidases in Bacillus subtilis
AU - Hashimoto, Masayuki
AU - Fujikura, Kentaro
AU - Miyake, Yukiko
AU - Higashitsuji, Yuhei
AU - Kiriyama, Yuuka
AU - Tanaka, Tatsuhito
AU - Yamamoto, Hiroki
AU - Sekiguchi, Junichi
N1 - Publisher Copyright:
© 2014 Japan Society for Bioscience, Biotechnology, and Agrochemistry.
PY - 2014
Y1 - 2014
N2 - The Gram-positive bacterium Bacillus subtilis has a thick cell wall. The cell wall contains various proteins, both for secretion and for peptidoglycan (PG) maintenance. Penicillin-binding proteins for PG synthesis, PG hydrolases (autolysins), and regulator proteins for the autolysins are the known components of the PG maintenance system. YqgA was identified as an abundant protein attached to the cell wall of B. subtilis through a proteomics analysis. The YqgA protein was localized at cell division sites during the transition period between the exponential and the stationary phases. YqgA localization was affected by mutations in the DL-endopeptidases (DLEPases), which are the autolysins involved in cell morphogenesis. Furthermore, yqgA mutations on a background of defective DLEPases led to delays in cell growth and cell morphological changes. These results demonstrate that yqgA is genetically related to the genes encoding DLEPases involved in cell morphogenesis.
AB - The Gram-positive bacterium Bacillus subtilis has a thick cell wall. The cell wall contains various proteins, both for secretion and for peptidoglycan (PG) maintenance. Penicillin-binding proteins for PG synthesis, PG hydrolases (autolysins), and regulator proteins for the autolysins are the known components of the PG maintenance system. YqgA was identified as an abundant protein attached to the cell wall of B. subtilis through a proteomics analysis. The YqgA protein was localized at cell division sites during the transition period between the exponential and the stationary phases. YqgA localization was affected by mutations in the DL-endopeptidases (DLEPases), which are the autolysins involved in cell morphogenesis. Furthermore, yqgA mutations on a background of defective DLEPases led to delays in cell growth and cell morphological changes. These results demonstrate that yqgA is genetically related to the genes encoding DLEPases involved in cell morphogenesis.
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U2 - 10.1080/09168451.2014.923294
DO - 10.1080/09168451.2014.923294
M3 - Article
C2 - 25130749
AN - SCOPUS:84928047676
SN - 0916-8451
VL - 78
SP - 1428
EP - 1434
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
IS - 8
ER -