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Identification of a novel transcriptional repressor (HEPIS) that interacts with nsp-10 of SARS coronavirus.

Identifieur interne : 001B17 ( PubMed/Checkpoint ); précédent : 001B16; suivant : 001B18

Identification of a novel transcriptional repressor (HEPIS) that interacts with nsp-10 of SARS coronavirus.

Auteurs : Min Hong [République populaire de Chine] ; Weizhong Li ; Lichun Wang ; Li Jiang ; Longding Liu ; Hongling Zhao ; Qihan Li

Source :

RBID : pubmed:18433331

Descripteurs français

English descriptors

Abstract

A novel gene was previously isolated from a cDNA library of human embryo lung tissue by its encoded protein, which interacts with non-structural protein 10 (nsp-10) of the severe acute respiratory syndrome coronavirus (SARS-CoV). The protein was named human embryo lung cellular protein interacting with SARS-CoV nsp-10 (HEPIS), and it is composed of 147 amino acids with several CK II phosphorylation sites. In the present study, we demonstrated that HEPIS was capable of suppressing chloramphenicol acetyltransferase (CAT) gene expression controlled by different enhancerelements in a transcription assay. HEPIS interacted specifically with the HSP70 TATA sequence, and not with various other enhancer elements in a binding test. Furthermore, we co-immunoprecipitated HEPIS with BTF3, a component of the RNA pol II initiation complex, and observed reduced proliferation of HeLa cells transfected with the HEPIS gene. Taken together, our results suggest that HEPIS may function as a potential transcriptional repressor.

DOI: 10.1089/vim.2007.0108
PubMed: 18433331


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pubmed:18433331

Le document en format XML

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<div type="abstract" xml:lang="en">A novel gene was previously isolated from a cDNA library of human embryo lung tissue by its encoded protein, which interacts with non-structural protein 10 (nsp-10) of the severe acute respiratory syndrome coronavirus (SARS-CoV). The protein was named human embryo lung cellular protein interacting with SARS-CoV nsp-10 (HEPIS), and it is composed of 147 amino acids with several CK II phosphorylation sites. In the present study, we demonstrated that HEPIS was capable of suppressing chloramphenicol acetyltransferase (CAT) gene expression controlled by different enhancerelements in a transcription assay. HEPIS interacted specifically with the HSP70 TATA sequence, and not with various other enhancer elements in a binding test. Furthermore, we co-immunoprecipitated HEPIS with BTF3, a component of the RNA pol II initiation complex, and observed reduced proliferation of HeLa cells transfected with the HEPIS gene. Taken together, our results suggest that HEPIS may function as a potential transcriptional repressor.</div>
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