RRC ID 3187
Author Ichimura T, Yamazoe M, Maeda M, Wada C, Hiraga S.
Title Proteolytic activity of YibP protein in Escherichia coli.
Journal J Bacteriol
Abstract Escherichia coli YibP protein (47.4 kDa) has a membrane-spanning signal at the N-terminal region, two long coiled-coil regions in the middle part, and a C-terminal globular domain, which involves amino acid sequences homologous to the peptidase M23/M37 family. A yibP disrupted mutant grows in rich medium at 37 degrees C but not at 42 degrees C. In the yibP null mutant, cell division and FtsZ ring formation are inhibited at 42 degrees C without SOS induction, resulting in filamentous cells with multiple nucleoids and finally in cell lysis. Five percent betaine suppresses the temperature sensitivity of the yibP disrupted mutation. The mutant has the same sensitivity to drugs, such as nalidixic acid, ethidium bromide, ethylmethane sulfonate, and sodium dodecyl sulfate, as the parental strain. YibP protein is recovered in the inner membrane and cytoplasmic fractions, but not in the outer membrane fraction. Results suggest that the coiled-coil regions and the C-terminal globular domain of YibP are localized in the cytoplasmic space, not in the periplasmic space. Purified YibP has a protease activity that split the substrate beta-casein.
Volume 184(10)
Pages 2595-602
Published 2002-5-1
DOI 10.1128/jb.184.10.2595-2602.2002
PMID 11976287
PMC PMC135028
MeSH Amino Acid Motifs Amino Acid Sequence Endopeptidases / chemistry* Escherichia coli Proteins / chemistry* Molecular Sequence Data Recombinant Fusion Proteins / analysis
IF 3.234
Times Cited 17
WOS Category MICROBIOLOGY
Resource
Prokaryotes E. coli ME7828(YK1100) ME9042(BL21(DE3)) DF264 ME8461(BD18) ME8279(CH1524) ME7813 ME7812
INFORMATION E.coli