当前位置： SCI文献检索 > BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS期刊下所有文献 > The acidic domain of hnRNPQ (NSAP1) has structural similarity to Barstar and binds to Apobec1.

The acidic domain of hnRNPQ (NSAP1) has structural similarity to Barstar and binds to Apobec1.

Abstract：

:Apobec1 edits the ApoB mRNA by deaminating nucleotide C(6666), 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 6xHis-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 6xHis-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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Quaresma AJ,Oyama S Jr,Barbosa JA,Kobarg J

doi

10.1016/j.bbrc.2006.09.044

subject

Has Abstract

pub_date

2006-11-17 00:00:00

pages

288-97

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(06)02058-4

journal_volume

350

pub_type

杂志文章

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