دورية أكاديمية

Cardiolipin synthase A colocalizes with cardiolipin and osmosensing transporter ProP at the poles of Escherichia coli cells

التفاصيل البيبلوغرافية
العنوان: Cardiolipin synthase A colocalizes with cardiolipin and osmosensing transporter ProP at the poles of Escherichia coli cells
المؤلفون: Romantsov, Tatyana, Gonzalez, Karen, Sahtout, Naheda, Culham, Doreen E., Coumoundouros, Chelsea, Garner, Jennifer, Kerr, Craig H., Chang, Limei, Turner, Raymond J., Wood, Janet M.
المساهمون: Natural Sciences and Engineering Research Council of Canada, Canadian Institutes of Health Research
المصدر: Molecular Microbiology ; volume 107, issue 5, page 623-638 ; ISSN 0950-382X 1365-2958
بيانات النشر: Wiley
سنة النشر: 2018
المجموعة: Wiley Online Library (Open Access Articles via Crossref)
الوصف: Summary Osmosensing by transporter ProP is modulated by its cardiolipin (CL)‐dependent concentration at the poles of Escherichia coli cells. Other contributors to this phenomenon were sought with the BACterial Two‐Hybrid System (BACTH). The BACTH‐tagged variants T18‐ProP and T25‐ProP retained ProP function and localization. Their interaction confirmed the ProP homo‐dimerization previously established by protein crosslinking. YdhP, YjbJ and ClsA were prominent among the putative ProP interactors identified by the BACTH system. The functions of YdhP and YjbJ are unknown, although YjbJ is an abundant, osmotically induced, soluble protein. ClsA (CL Synthase A) had been shown to determine ProP localization by mediating CL synthesis. Unlike a deletion of clsA , deletion of ydhP or yjbJ had no effect on ProP localization or function. All three proteins were concentrated at the cell poles, but only ClsA localization was CL‐dependent. ClsA was shown to be N‐terminally processed and membrane‐anchored, with dual, cytoplasmic, catalytic domains. Active site amino acid replacements (H224A plus H404A) inactivated ClsA and compromised ProP localization. YdhP and YjbJ may be ClsA effectors, and interactions of YdhP, YjbJ and ClsA with ProP may reflect their colocalization at the cell poles. Targeted CL synthesis may contribute to the polar localization of CL, ClsA and ProP.
نوع الوثيقة: article in journal/newspaper
اللغة: English
DOI: 10.1111/mmi.13904
الإتاحة: https://doi.org/10.1111/mmi.13904Test
حقوق: http://onlinelibrary.wiley.com/termsAndConditions#vorTest
رقم الانضمام: edsbas.D24B3AA7
قاعدة البيانات: BASE