کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1940487 1050782 2006 10 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
The acidic domain of hnRNPQ (NSAP1) has structural similarity to Barstar and binds to Apobec1
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
The acidic domain of hnRNPQ (NSAP1) has structural similarity to Barstar and binds to Apobec1
چکیده انگلیسی

Apobec1 edits the ApoB mRNA by deaminating nucleotide C6666, which results in a codon change from Glutamate to stop, and subsequent expression of a truncated protein. Apobec1 is regulated by ACF (Apobec1 complementation factor) and hnRNPQ, which contains an N-terminal “acidic domain” (AcD) of unknown function, three RNA recognition motifs, and an Arg/Gly-rich region. Here, we modeled the structure of AcD using the bacterial protein Barstar as a template. Furthermore, we demonstrated by in vitro pull-down assays that 6×His-AcD alone is able to interact with GST–Apobec1. Finally, we performed in silico phosphorylation of AcD and molecular dynamics studies, which indicate conformational changes in the phosphorylated form. The results of the latter studies were confirmed by in vitro phosphorylation of 6×His-AcD by protein kinase C, mass spectrometry, and spectroscopic analyses. Our data suggest hnRNPQ interactions via its AcD with Apobec1 and that this interaction is regulated by the AcD phosphorylation.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 350, Issue 2, 17 November 2006, Pages 288–297
نویسندگان
, , , ,