Comparative structural and functional analysis of the glycine-rich regions of Class A and B J-domain protein cochaperones of Hsp70.

التفاصيل البيبلوغرافية
العنوان: Comparative structural and functional analysis of the glycine-rich regions of Class A and B J-domain protein cochaperones of Hsp70.
المؤلفون: Ciesielski, Szymon J, Schilke, Brenda A, Stolarska, Milena, Tonelli, Marco, Tomiczek, Bartlomiej, Craig, Elizabeth A
المصدر: FEBS Lett ; ISSN:1873-3468 ; Volume:598 ; Issue:12
بيانات النشر: Wiley
سنة النشر: 2024
المجموعة: PubMed Central (PMC)
مصطلحات موضوعية: Hsp40, JDP, J‐domain, heat shock protein, molecular chaperone, protein homeostasis
الوصف: J-domain proteins are critical Hsp70 co-chaperones. A and B types have a poorly understood glycine-rich region (Grich) adjacent to their N-terminal J-domain (Jdom). We analyzed the ability of Jdom/Grich segments of yeast Class B Sis1 and a suppressor variant of Class A, Ydj1, to rescue the inviability of sis1-∆. In each, we identified a cluster of Grich residues required for rescue. Both contain conserved hydrophobic and acidic residues and are predicted to form helices. While, as expected, the Sis1 segment docks on its J-domain, that of Ydj1 does not. However, data suggest both interact with Hsp70. We speculate that the Grich-Hsp70 interaction of Classes A and B J-domain proteins can fine tune the activity of Hsp70, thus being particularly important for the function of Class B.
نوع الوثيقة: report
article in journal/newspaper
اللغة: English
العلاقة: https://doi.org/10.1002/1873-3468.14857Test; https://pubmed.ncbi.nlm.nih.gov/38529663Test; https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11209805Test/
DOI: 10.1002/1873-3468.14857
الإتاحة: https://doi.org/10.1002/1873-3468.14857Test
https://pubmed.ncbi.nlm.nih.gov/38529663Test
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11209805Test/
حقوق: © 2024 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.
رقم الانضمام: edsbas.60AA2357
قاعدة البيانات: BASE