Penicillin-binding protein 2x of Streptococcus pneumoniae: the mutation Ala707Asp within the C-terminal PASTA2 domain leads to destabilization.
Penicillin-binding protein 2x of Streptococcus pneumoniae: the mutation Ala707Asp within the C-terminal PASTA2 domain leads to destabilization.
复制标题
肺炎链球菌青霉素结合蛋白 2x:C 端 PASTA2 结构域内的 Ala707Asp 突变导致不稳定
DOI:
10.1089/mdr.2014.0082
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发表时间:
2014
影响因子:
2.6
通讯作者:
D. Denapaite
中科院分区:
文献类型:
--
作者:
Schweizer;K. Peters;C. Stahlmann;R. Hakenbeck;D. Denapaite
Streptococcus pneumoniaepenicillin-binding protein 2x (PBP2x) is an enzyme involved in the last stages of peptidoglycan assembly and essential for bacterial growth and survival. PBP2x localizes to the division site, a process that depends on itsPenicillin-Binding ProteinAndSerine-Threonine-kinaseAssociated (PASTA) domains, which was previously demonstrated via GFP-PBP2x in living cells. During this study a mutant strain was isolated in which the GFP-PBP2x fusion protein did not localize at division sites and it contained reduced amounts of the full-length GFP-PBP2x. We now show that this defect is due to a point mutation within the C-terminal PASTA2 domain of PBP2x. The mutant protein was analyzed in detail in terms of beta-lactam binding, functionality, and localization in live cells. We demonstrate that the mutation affects the GFP-tagged PBP2x variant severely and renders it susceptible to the protease/chaperone HtrA.
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影响因子:
3.6
作者:
Geneviève Alioing;Chantal Granadel;D. Morrison;J. Claverys
通讯作者:
J. Claverys
影响因子:
3.6
作者:
Morlot, C.;Bayle, L.;Di Guilmi, A. M.
通讯作者:
Di Guilmi, A. M.
DOI:
10.1084/jem.116.4.491
发表时间:
1962-10-01
期刊:
The Journal of experimental medicine
影响因子:
--
作者:
OTTOLENGHI E;HOTCHKISS RD
通讯作者:
HOTCHKISS RD
影响因子:
3.2
作者:
Paik, J;Kern, I;Hakenbeck, R
通讯作者:
Hakenbeck, R
影响因子:
4.8
作者:
Dessen, A;Mouz, N;Dideberg, O
通讯作者:
Dideberg, O