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DNA damage response signaling does not trigger redistribution of SAMHD1 to nuclear foci.

Abstract：

:SAMHD1 (Sterile alpha motif and histidine-aspartic acid (HD) domain containing protein 1) is a deoxyribonucleoside triphosphate (dNTP) triphosphohydrolase (dNTPase) that restricts viral replication in infected cells. This protein is also involved in DNA repair by assisting in DNA end resection by homologous recombination (HR) after DNA double-strand break (DSB) induction with camptothecin (CPT) or etoposide (ETO). We showed that a monoclonal anti-SAMHD1 antibody produced against the full-length protein detected an unspecific 50 kDa protein that colocalized with dot-like structures after CPT treatment in HeLa cells. In contrast, a polyclonal anti-SAMHD1 antibody raised against the N-terminus of this protein specifically detected SAMHD1, as shown in Jurkat, HAP1KO and HEK293T SAMHD1-siRNA cell lysates compared with their respective controls. Our findings showed that SAMHD1 is not localized in dot-like structures under DSB induction in HeLa cells.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Medeiros AC,Soares CS,Coelho PO,Vieira NA,Baqui MMA,Teixeira FR,Gomes MD

doi

10.1016/j.bbrc.2018.03.225

subject

Has Abstract

pub_date

2018-05-23 00:00:00

pages

790-796

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(18)30758-7

journal_volume

499

pub_type

杂志文章

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