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A proteomic study of TAR-RNA binding protein (TRBP)-associated factors

BACKGROUND: The human TAR RNA-binding protein, TRBP, was first identified and cloned based on its high affinity binding to the small hairpin trans-activation responsive (TAR) RNA of HIV-1. TRBP has more recently been found to be a constituent of the RNA-induced silencing complex (RISC) serving as a...

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Autores principales: Chi, Ya-Hui, Semmes, Oliver John, Jeang, Kuan-Teh
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3125213/
https://www.ncbi.nlm.nih.gov/pubmed/21711701
http://dx.doi.org/10.1186/2045-3701-1-9
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author Chi, Ya-Hui
Semmes, Oliver John
Jeang, Kuan-Teh
author_facet Chi, Ya-Hui
Semmes, Oliver John
Jeang, Kuan-Teh
author_sort Chi, Ya-Hui
collection PubMed
description BACKGROUND: The human TAR RNA-binding protein, TRBP, was first identified and cloned based on its high affinity binding to the small hairpin trans-activation responsive (TAR) RNA of HIV-1. TRBP has more recently been found to be a constituent of the RNA-induced silencing complex (RISC) serving as a Dicer co-factor in the processing of the ~70 nucleotide pre-microRNAs(miRNAs) to 21-25 nucleotide mature miRNAs. FINDINGS: Using co-immunoprecipitation and protein-identification by mass spectrometry, we characterized intracellular proteins that complex with TRBP. These interacting proteins include those that have been described to act in protein synthesis, RNA modifications and processing, DNA transcription, and cell proliferation. CONCLUSIONS: Our findings provide a proteome of factors that may cooperate with TRBP in activities such as miRNA processing and in RNA interference by the RISC complex.
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spelling pubmed-31252132011-06-29 A proteomic study of TAR-RNA binding protein (TRBP)-associated factors Chi, Ya-Hui Semmes, Oliver John Jeang, Kuan-Teh Cell Biosci Short Report BACKGROUND: The human TAR RNA-binding protein, TRBP, was first identified and cloned based on its high affinity binding to the small hairpin trans-activation responsive (TAR) RNA of HIV-1. TRBP has more recently been found to be a constituent of the RNA-induced silencing complex (RISC) serving as a Dicer co-factor in the processing of the ~70 nucleotide pre-microRNAs(miRNAs) to 21-25 nucleotide mature miRNAs. FINDINGS: Using co-immunoprecipitation and protein-identification by mass spectrometry, we characterized intracellular proteins that complex with TRBP. These interacting proteins include those that have been described to act in protein synthesis, RNA modifications and processing, DNA transcription, and cell proliferation. CONCLUSIONS: Our findings provide a proteome of factors that may cooperate with TRBP in activities such as miRNA processing and in RNA interference by the RISC complex. BioMed Central 2011-02-25 /pmc/articles/PMC3125213/ /pubmed/21711701 http://dx.doi.org/10.1186/2045-3701-1-9 Text en Copyright ©2011 Chi et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Short Report
Chi, Ya-Hui
Semmes, Oliver John
Jeang, Kuan-Teh
A proteomic study of TAR-RNA binding protein (TRBP)-associated factors
title A proteomic study of TAR-RNA binding protein (TRBP)-associated factors
title_full A proteomic study of TAR-RNA binding protein (TRBP)-associated factors
title_fullStr A proteomic study of TAR-RNA binding protein (TRBP)-associated factors
title_full_unstemmed A proteomic study of TAR-RNA binding protein (TRBP)-associated factors
title_short A proteomic study of TAR-RNA binding protein (TRBP)-associated factors
title_sort proteomic study of tar-rna binding protein (trbp)-associated factors
topic Short Report
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3125213/
https://www.ncbi.nlm.nih.gov/pubmed/21711701
http://dx.doi.org/10.1186/2045-3701-1-9
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