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SR 蛋白家族。

The SR protein family.

机构信息

Department of Microbiology and Molecular Genetics, University of California, Irvine, Irvine, CA 92697-4025, USA.

出版信息

Genome Biol. 2009;10(10):242. doi: 10.1186/gb-2009-10-10-242. Epub 2009 Oct 27.

DOI:10.1186/gb-2009-10-10-242
PMID:19857271
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2784316/
Abstract

The processing of pre-mRNAs is a fundamental step required for the expression of most metazoan genes. Members of the family of serine/arginine (SR)-rich proteins are critical components of the machineries carrying out these essential processing events, highlighting their importance in maintaining efficient gene expression. SR proteins are characterized by their ability to interact simultaneously with RNA and other protein components via an RNA recognition motif (RRM) and through a domain rich in arginine and serine residues, the RS domain. Their functional roles in gene expression are surprisingly diverse, ranging from their classical involvement in constitutive and alternative pre-mRNA splicing to various post-splicing activities, including mRNA nuclear export, nonsense-mediated decay, and mRNA translation. These activities point up the importance of SR proteins during the regulation of mRNA metabolism.

摘要

前体 mRNA 的加工是大多数后生动物基因表达所必需的基本步骤。丝氨酸/精氨酸(SR)丰富蛋白家族的成员是执行这些基本加工事件的机器的关键组成部分,这突出了它们在维持有效基因表达方面的重要性。SR 蛋白的特点是能够通过 RNA 识别基序(RRM)和富含精氨酸和丝氨酸残基的 RS 结构域,同时与 RNA 和其他蛋白质成分相互作用。它们在基因表达中的功能作用非常多样化,从它们在组成型和选择性前体 mRNA 剪接中的经典参与到各种剪接后活性,包括 mRNA 核输出、无意义介导的衰变和 mRNA 翻译。这些活性表明了 SR 蛋白在 mRNA 代谢调控中的重要性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/402c/2784316/ef38278f104a/gb-2009-10-10-242-6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/402c/2784316/385119d5afd2/gb-2009-10-10-242-1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/402c/2784316/131a2cbfe44a/gb-2009-10-10-242-2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/402c/2784316/1494686994cf/gb-2009-10-10-242-3.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/402c/2784316/196837c9d3d0/gb-2009-10-10-242-5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/402c/2784316/ef38278f104a/gb-2009-10-10-242-6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/402c/2784316/385119d5afd2/gb-2009-10-10-242-1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/402c/2784316/131a2cbfe44a/gb-2009-10-10-242-2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/402c/2784316/1494686994cf/gb-2009-10-10-242-3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/402c/2784316/0ff5759cdc3e/gb-2009-10-10-242-4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/402c/2784316/196837c9d3d0/gb-2009-10-10-242-5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/402c/2784316/ef38278f104a/gb-2009-10-10-242-6.jpg

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Co-evolution of the branch site and SR proteins in eukaryotes.真核生物中分支位点与SR蛋白的共同进化。
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Viral Modulation of Host Splicing.病毒对宿主剪接的调控
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LincRNA-ASAO promotes dental pulp repair through interacting with PTBP1 to increase ALPL alternative splicing.长链非编码RNA-ASAO通过与PTBP1相互作用促进牙髓修复,以增加碱性磷酸酶(ALPL)的可变剪接。
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