TY - JOUR
T1 - Functional analysis of the secretory precursor processing machinery of Bacillus subtilis
T2 - Identification of a eubacterial homolog of archaeal and eukaryotic signal peptidases
AU - Tjalsma, Harold
AU - Bolhuis, Albert
AU - Van Roosmalen, Maarten L.
AU - Wiegert, Thomas
AU - Schumann, Wolfgang
AU - Broekhuizen, Cees P.
AU - Quax, Wim J.
AU - Venema, Gerard
AU - Bron, Sierd
AU - Van Dijl, Jan Maarten
PY - 1998/8/1
Y1 - 1998/8/1
N2 - Approximately 47% of the genes of the Gram-positive bacterium Bacillus subtilis belong to paralogous gene families. The present studies were aimed at the functional analysis of the sip gene family of B. subtilis, consisting of five chromosomal genes, denoted sipS, sipT, sipU, sipV, and sipW. All five sip genes specify type I signal peptidases (SPases), which are actively involved in the processing of secretory preproteins. Interestingly, strains lacking as many as four of these SPases could be obtained. As shown with a temperature-sensitive SipS variant, only cells lacking both SipS and SipT were not viable, which may be caused by jamming of the secretion machinery with secretory preproteins. Thus, SipS and SipT are of major importance for protein secretion. This conclusion is underscored by the observation that only the transcription of the sips and sipT genes is temporally controlled via the DegS-DegU regulatory system, in concert with the transcription of most genes for secretory preproteins. Notably, the newly identified SPase SipW is highly similar to SPases from archaea and the ER membrane of eukaryotes, suggesting that these enzymes form a subfamily of the type I SPases, which is conserved in the three domains of life.
AB - Approximately 47% of the genes of the Gram-positive bacterium Bacillus subtilis belong to paralogous gene families. The present studies were aimed at the functional analysis of the sip gene family of B. subtilis, consisting of five chromosomal genes, denoted sipS, sipT, sipU, sipV, and sipW. All five sip genes specify type I signal peptidases (SPases), which are actively involved in the processing of secretory preproteins. Interestingly, strains lacking as many as four of these SPases could be obtained. As shown with a temperature-sensitive SipS variant, only cells lacking both SipS and SipT were not viable, which may be caused by jamming of the secretion machinery with secretory preproteins. Thus, SipS and SipT are of major importance for protein secretion. This conclusion is underscored by the observation that only the transcription of the sips and sipT genes is temporally controlled via the DegS-DegU regulatory system, in concert with the transcription of most genes for secretory preproteins. Notably, the newly identified SPase SipW is highly similar to SPases from archaea and the ER membrane of eukaryotes, suggesting that these enzymes form a subfamily of the type I SPases, which is conserved in the three domains of life.
KW - Bacillus subtilis
KW - Leader peptidase
KW - Paralogous gene family
KW - Protein secretion
KW - Signal peptidase
UR - http://www.scopus.com/inward/record.url?scp=0032146073&partnerID=8YFLogxK
U2 - 10.1101/gad.12.15.2318
DO - 10.1101/gad.12.15.2318
M3 - Article
C2 - 9694797
AN - SCOPUS:0032146073
VL - 12
SP - 2318
EP - 2331
JO - Genes & Development
JF - Genes & Development
SN - 0890-9369
IS - 15
ER -