原创力文档replication protein a (rpa) hampers the processive action of apobec3g cytosine deaminase on single-stranded dna复制的蛋白质(战)阻碍前进的行动apobec3g单链dna胞嘧啶脱氨酶.pdfVIP
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replication protein a (rpa) hampers the processive action of apobec3g cytosine deaminase on single-stranded dna复制的蛋白质(战)阻碍前进的行动apobec3g单链dna胞嘧啶脱氨酶
Replication Protein A (RPA) Hampers the Processive
Action of APOBEC3G Cytosine Deaminase on
Single-Stranded DNA
1 1. 1. 1¤
Artem G. Lada , Irina S.-R. Waisertreiger , Corinn E. Grabow , Aishwarya Prakash , Gloria E. O.
1 2,3 1
Borgstahl , Igor B. Rogozin , Youri I. Pavlov *
1 Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska, United States of America, 2 National Center for
Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, Maryland, United States of America, 3 Institute of Cytology and Genetics,
Novosibirsk, Russia
Abstract
Background: Editing deaminases have a pivotal role in cellular physiology. A notable member of this superfamily,
APOBEC3G (A3G), restricts retroviruses, and Activation Induced Deaminase (AID) generates antibody diversity by localized
deamination of cytosines in DNA. Unconstrained deaminase activity can cause genome-wide mutagenesis and cancer. The
mechanisms that protect the genomic DNA from the undesired action of deaminases are unknown. Using the in vitro
deamination assays and expression of A3G in yeast, we show that replication protein A (RPA), the eukaryotic single-stranded
DNA (ssDNA) binding protein, severely inhibits the deamination activity and processivity of A3G.
Principal Findings/Methodology: We found that mutations induced by A3G in the yeast genomic reporter are changes of a
single nucleotide. This is unexpected because of the known property of A3G to catalyze multiple deaminations upon one
substrate encounter event in vitro. The addition of
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