The structure of the mRNA export factor TAP reveals a cis arrangement of a non-canonical RNP domain and an LRR domain

Human TAP is implicated in mRNA nuclear export and is used by simian type D retroviruses to export their unspliced genomic RNA to the cytoplasm of the host cell. We have determined the crystal structure of the minimal TAP fragment that binds the constitutive transport element (CTE) of retroviral RNA...

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Hlavní autoři: Liker, Erika, Fernandez, Elena, Izaurralde, Elisa, Conti, Elena
Médium: Artigo
Jazyk:Inglês
Vydáno: Oxford University Press 2000
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On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC305804/
https://ncbi.nlm.nih.gov/pubmed/11060011
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/emboj/19.21.5587
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spelling pubmed-3058042004-04-08 The structure of the mRNA export factor TAP reveals a cis arrangement of a non-canonical RNP domain and an LRR domain Liker, Erika Fernandez, Elena Izaurralde, Elisa Conti, Elena EMBO J Articles Human TAP is implicated in mRNA nuclear export and is used by simian type D retroviruses to export their unspliced genomic RNA to the cytoplasm of the host cell. We have determined the crystal structure of the minimal TAP fragment that binds the constitutive transport element (CTE) of retroviral RNAs. Unexpectedly, we find the fragment consists of a ribonucleoprotein (RNP) domain, which is not identifiable by its sequence, and a leucine-rich repeat (LRR) domain. The non-canonical RNP domain functions as the general RNA-binding portion of the fragment. The LRR domain is required in cis to the RNP domain for CTE RNA binding. The structural and biochemical properties of the domains point to a remarkable similarity with the U2B′′(RNP)–U2A′(LRR) spliceosomal heterodimer. Our in vitro and in vivo functional studies using structure-based mutants suggest that a phylogenetically conserved surface of the LRR domain of TAP may have different roles in the export of viral and cellular RNAs. Oxford University Press 2000-11-01 /pmc/articles/PMC305804/ /pubmed/11060011 http://dx.doi.org/10.1093/emboj/19.21.5587 Text en Copyright © 2000 European Molecular Biology Organization
institution US NLM
collection PubMed Central
language Inglês
format Artigo
topic Articles
spellingShingle Articles
Liker, Erika
Fernandez, Elena
Izaurralde, Elisa
Conti, Elena
The structure of the mRNA export factor TAP reveals a cis arrangement of a non-canonical RNP domain and an LRR domain
description Human TAP is implicated in mRNA nuclear export and is used by simian type D retroviruses to export their unspliced genomic RNA to the cytoplasm of the host cell. We have determined the crystal structure of the minimal TAP fragment that binds the constitutive transport element (CTE) of retroviral RNAs. Unexpectedly, we find the fragment consists of a ribonucleoprotein (RNP) domain, which is not identifiable by its sequence, and a leucine-rich repeat (LRR) domain. The non-canonical RNP domain functions as the general RNA-binding portion of the fragment. The LRR domain is required in cis to the RNP domain for CTE RNA binding. The structural and biochemical properties of the domains point to a remarkable similarity with the U2B′′(RNP)–U2A′(LRR) spliceosomal heterodimer. Our in vitro and in vivo functional studies using structure-based mutants suggest that a phylogenetically conserved surface of the LRR domain of TAP may have different roles in the export of viral and cellular RNAs.
author Liker, Erika
Fernandez, Elena
Izaurralde, Elisa
Conti, Elena
author_facet Liker, Erika
Fernandez, Elena
Izaurralde, Elisa
Conti, Elena
author_sort Liker, Erika
title The structure of the mRNA export factor TAP reveals a cis arrangement of a non-canonical RNP domain and an LRR domain
title_short The structure of the mRNA export factor TAP reveals a cis arrangement of a non-canonical RNP domain and an LRR domain
title_full The structure of the mRNA export factor TAP reveals a cis arrangement of a non-canonical RNP domain and an LRR domain
title_fullStr The structure of the mRNA export factor TAP reveals a cis arrangement of a non-canonical RNP domain and an LRR domain
title_full_unstemmed The structure of the mRNA export factor TAP reveals a cis arrangement of a non-canonical RNP domain and an LRR domain
title_sort structure of the mrna export factor tap reveals a cis arrangement of a non-canonical rnp domain and an lrr domain
publisher Oxford University Press
publishDate 2000
url https://ncbi.nlm.nih.gov/pmc/articles/PMC305804/
https://ncbi.nlm.nih.gov/pubmed/11060011
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/emboj/19.21.5587
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