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

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 unkno...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2006-11, Vol.350 (2), p.288-297
Main Authors: Quaresma, Alexandre J.C., Oyama, Sergio, Barbosa, João A.R.G., Kobarg, Jörg
Format: Article
Language:English
Subjects:
AcD domain
Amino Acid Sequence
APOBEC-1 Deaminase
Apobec1
Bacterial Proteins - chemistry
Binding Sites
Circular Dichroism
Computer Simulation
Cytidine Deaminase - metabolism
Heterogeneous-Nuclear Ribonucleoproteins - chemistry
Heterogeneous-Nuclear Ribonucleoproteins - metabolism
Histidine - metabolism
hnRNPQ/NSAP1
Humans
Models, Molecular
Molecular dynamics
Molecular modeling
Molecular Sequence Data
Phosphorylation
Protein Kinase C - metabolism
Protein Structure, Tertiary
Protein–protein interactions
RNA editing
RNA-Binding Proteins - chemistry
Sequence Alignment
Serine - metabolism
Spectrometry, Fluorescence
Structural Homology, Protein
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Summary: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 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.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2006.09.044