کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1980439 1061856 2010 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Crosstalk between replicative and translesional DNA polymerases: PDIP38 interacts directly with Polη
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Crosstalk between replicative and translesional DNA polymerases: PDIP38 interacts directly with Polη
چکیده انگلیسی

Replicative DNA polymerases duplicate genomes in a very efficient and accurate mode. However their progression can be blocked by DNA lesions since they are unable to accommodate bulky damaged bases in their active site. In response to replication blockage, monoubiquitination of PCNA promotes the switch between replicative and specialized polymerases proficient to overcome the obstacle. In this study, we characterize novel connections between proteins involved in replication and TransLesion Synthesis (TLS). We demonstrate that PDIP38 (Polδ interacting protein of 38 kDa) directly interacts with the TLS polymerase Polη. Interestingly, the region of Polη interacting with PDIP38 is found to be located within the ubiquitin-binding zinc finger domain (UBZ) of Polη. We show that the depletion of PDIP38 increases the number of cells with Polη foci in the absence of DNA damage and diminishes cell survival after UV irradiation. In addition, PDIP38 is able to interact directly not only with Polη but also with the specialized polymerases Rev1 and Polζ (via Rev7). We thus suggest that PDIP38 serves as a mediator protein helping TLS Pols to transiently replace replicative polymerases at damaged sites.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: DNA Repair - Volume 9, Issue 8, 5 August 2010, Pages 922–928
نویسندگان
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