Bacillus licheniformis BlaR1 L3 loop is a zinc metalloprotease activated by self-proteolysis.
Bacillus licheniformis BlaR1 L3 loop is a zinc metalloprotease activated by self-proteolysis.
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DOI:
10.1371/journal.pone.0036400
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发表时间:
2012
期刊:
影响因子:
3.7
通讯作者:
Joris B
中科院分区:
文献类型:
--
作者:
Berzigotti S;Benlafya K;Sépulchre J;Amoroso A;Joris B
In Bacillus licheniformis 749/I, BlaP β-lactamase is induced by the presence of a β-lactam antibiotic outside the cell. The first step in the induction mechanism is the detection of the antibiotic by the membrane-bound penicillin receptor BlaR1 that is composed of two functional domains: a carboxy-terminal domain exposed outside the cell, which acts as a penicillin sensor, and an amino-terminal domain anchored to the cytoplasmic membrane, which works as a transducer-transmitter. The acylation of BlaR1 sensor domain by the antibiotic generates an intramolecular signal that leads to the activation of the L3 cytoplasmic loop of the transmitter by a single-point cleavage. The exact mechanism of L3 activation and the nature of the secondary cytoplasmic signal launched by the activated transmitter remain unknown. However, these two events seem to be linked to the presence of a HEXXH zinc binding motif of neutral zinc metallopeptidases. By different experimental approaches, we demonstrated that the L3 loop binds zinc ion, belongs to Gluzincin metallopeptidase superfamily and is activated by self-proteolysis.
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影响因子:
4.1
作者:
MATAGNE, A;MISSELYNBAUDUIN, AM;FRERE, JM
通讯作者:
FRERE, JM
影响因子:
3.6
作者:
Filée, P;Benlafya, K;Joris, B
通讯作者:
Joris, B
影响因子:
3.6
作者:
Hardt, K;Joris, B;Ghuysen, JM
通讯作者:
Ghuysen, JM
影响因子:
3.2
作者:
KOBAYASHI, T;ZHU, YF;LAMPEN, JO
通讯作者:
LAMPEN, JO
DOI:
10.1073/pnas.1005681107
发表时间:
2010-10-12
影响因子:
11.1
作者:
Gao, Xiang;Wang, Jue;Zhang, Yu-Zhong
通讯作者:
Zhang, Yu-Zhong