Abstract
SpoIVB is essential for intercompartmental signalling in the s(K)-checkpoint of Bacillus subtilis. SpoIVB is synthesized in the spore chamber and is the signal which activates proteolytic processing of pro-s(K) to its mature and active form s(K). We show here that SpoIVB is a serine peptidase of the SA clan. Expression of SpoIVB in Escherichia coli has shown that SpoIVB is able to self-cleave into at least three discrete products, and in vitro studies have shown cleavage in trans. Autoproteolysis of SpoIVB is tightly linked to the initiation of the two developmental functions of this protein, signalling of pro-s(K) processing and a yet, uncharacterized, second function which is essential for the formation of heat-resistant spores. In B. subtilis, SpoIVB is synthesized as a zymogen and is subject to two levels of proteolysis. First, autoproteolysis generating intermediate products, at least one of which is proposed to be the active form, followed by processing by one or more enzymes to smaller species. This could provide a mechanism for switching off the active SpoIVB intermediate(s) and suggests a similarity to other proteolytic cascades such as those found in blood coagulation.
| Original language | English |
|---|---|
| Pages (from-to) | 1336-1348 |
| Number of pages | 13 |
| Journal | Molecular Microbiology |
| Volume | 36 |
| Issue number | 6 |
| DOIs | |
| Publication status | Published - 2000 |
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Proteolysis of SpoIVB is a critical determinant in signalling of Pro-σ(K) processing in Bacillus subtilis. / Wakeley, Philip R.; Dorazi, Robert; Hoa, Ngo Thi; Bowyer, John R.; Cutting, Simon M.
In: Molecular Microbiology, Vol. 36, No. 6, 2000, p. 1336-1348.Research output: Contribution to journal › Article
TY - JOUR
T1 - Proteolysis of SpoIVB is a critical determinant in signalling of Pro-σ(K) processing in Bacillus subtilis
AU - Wakeley, Philip R.
AU - Dorazi, Robert
AU - Hoa, Ngo Thi
AU - Bowyer, John R.
AU - Cutting, Simon M.
PY - 2000
Y1 - 2000
N2 - SpoIVB is essential for intercompartmental signalling in the s(K)-checkpoint of Bacillus subtilis. SpoIVB is synthesized in the spore chamber and is the signal which activates proteolytic processing of pro-s(K) to its mature and active form s(K). We show here that SpoIVB is a serine peptidase of the SA clan. Expression of SpoIVB in Escherichia coli has shown that SpoIVB is able to self-cleave into at least three discrete products, and in vitro studies have shown cleavage in trans. Autoproteolysis of SpoIVB is tightly linked to the initiation of the two developmental functions of this protein, signalling of pro-s(K) processing and a yet, uncharacterized, second function which is essential for the formation of heat-resistant spores. In B. subtilis, SpoIVB is synthesized as a zymogen and is subject to two levels of proteolysis. First, autoproteolysis generating intermediate products, at least one of which is proposed to be the active form, followed by processing by one or more enzymes to smaller species. This could provide a mechanism for switching off the active SpoIVB intermediate(s) and suggests a similarity to other proteolytic cascades such as those found in blood coagulation.
AB - SpoIVB is essential for intercompartmental signalling in the s(K)-checkpoint of Bacillus subtilis. SpoIVB is synthesized in the spore chamber and is the signal which activates proteolytic processing of pro-s(K) to its mature and active form s(K). We show here that SpoIVB is a serine peptidase of the SA clan. Expression of SpoIVB in Escherichia coli has shown that SpoIVB is able to self-cleave into at least three discrete products, and in vitro studies have shown cleavage in trans. Autoproteolysis of SpoIVB is tightly linked to the initiation of the two developmental functions of this protein, signalling of pro-s(K) processing and a yet, uncharacterized, second function which is essential for the formation of heat-resistant spores. In B. subtilis, SpoIVB is synthesized as a zymogen and is subject to two levels of proteolysis. First, autoproteolysis generating intermediate products, at least one of which is proposed to be the active form, followed by processing by one or more enzymes to smaller species. This could provide a mechanism for switching off the active SpoIVB intermediate(s) and suggests a similarity to other proteolytic cascades such as those found in blood coagulation.
UR - http://www.scopus.com/inward/record.url?scp=0034199342&partnerID=8YFLogxK
U2 - 10.1046/j.1365-2958.2000.01946.x
DO - 10.1046/j.1365-2958.2000.01946.x
M3 - Article
VL - 36
SP - 1336
EP - 1348
JO - Molecular Microbiology
JF - Molecular Microbiology
SN - 0950-382X
IS - 6
ER -