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Penicillin-binding protein 2x of Streptococcus pneumoniae: the mutation Ala707Asp within the C-terminal PASTA2 domain leads to destabilization.

Lookup NU author(s): Dr Katharina Pazos Don Pedro

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Abstract

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 its Penicillin-Binding Protein And Serine-Threonine-kinase Associated (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.


Publication metadata

Author(s): Schweizer I, Peters K, Stahlmann C, Hakenbeck R, Denapaite D

Publication type: Article

Publication status: Published

Journal: Microbial Drug Resistance

Year: 2014

Volume: 20

Issue: 3

Pages: 250-257

Print publication date: 04/06/2014

Online publication date: 19/05/2014

Acceptance date: 19/05/2014

ISSN (print): 1076-6294

ISSN (electronic): 1931-8448

Publisher: Mary Ann Liebert, Inc. Publishers

URL: http://dx.doi.org/10.1089/mdr.2014.0082

DOI: 10.1089/mdr.2014.0082


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