FLASH Is Required for the Endonucleolytic Cleavage of Histone Pre-mRNAs but Is Dispensable for the 5′ Exonucleolytic Degradation of the Downstream Cleavage Product

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Published inMolecular and Cellular Biology Vol. 31; no. 7; pp. 1492 - 1502
Main Authors Yang, Xiao-cui, Xu, Bing, Sabath, Ivan, Kunduru, Lalitha, Burch, Brandon D., Marzluff, William F., Dominski, Zbigniew
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.04.2011
Taylor & Francis
Subjects
Amino Acid Sequence
Apoptosis Regulatory Proteins - chemistry
Apoptosis Regulatory Proteins - metabolism
Base Sequence
Binding Sites
Calcium-Binding Proteins - chemistry
Calcium-Binding Proteins - metabolism
DNA Mutational Analysis
Endonucleases - metabolism
Exonucleases - metabolism
Histones - genetics
Histones - metabolism
Humans
Models, Biological
Molecular Sequence Data
Protein Binding
Protein Interaction Mapping
Ribonucleoprotein, U7 Small Nuclear - metabolism
RNA Precursors - metabolism
RNA Processing, Post-Transcriptional
RNA-Binding Proteins - metabolism
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Abstract Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue MCB About MCB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy MCB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0270-7306 Online ISSN: 1098-5549 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to MCB .asm.org, visit: MCB       
AbstractList 3′-end cleavage of histone pre-mRNAs is catalyzed by CPSF-73 and requires the interaction of two U7 snRNP-associated proteins, FLASH and Lsm11. Here, by using scanning mutagenesis we identify critical residues in human FLASH and Lsm11 that are involved in the interaction between these two proteins. We also demonstrate that mutations in the region of FLASH located between amino acids 50 and 99 do not affect binding of Lsm11. Interestingly, these mutations convert FLASH into an inhibitory protein that reduces in vitro processing efficiency of highly active nuclear extracts. Our results suggest that this region in FLASH in conjunction with Lsm11 is involved in recruiting a yet-unknown processing factor(s) to histone pre-mRNA. Following endonucleolytic cleavage of histone pre-mRNA, the downstream cleavage product (DCP) is degraded by the 5′-3′ exonuclease activity of CPSF-73, which also depends on Lsm11. Strikingly, while cleavage of histone pre-mRNA is stimulated by FLASH and inhibited by both dominant negative mutants of FLASH and anti-FLASH antibodies, the 5′-3′ degradation of the DCP is not affected. Thus, the recruitment of FLASH to the processing complex plays a critical role in activating the endonuclease mode of CPSF-73 but is dispensable for its 5′-3′ exonuclease activity. These results suggest that CPSF-73, the catalytic component in both reactions, can be recruited to histone pre-mRNA largely in a manner independent of FLASH, possibly by a separate domain in Lsm11.
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3′-end cleavage of histone pre-mRNAs is catalyzed by CPSF-73 and requires the interaction of two U7 snRNP-associated proteins, FLASH and Lsm11. Here, by using scanning mutagenesis we identify critical residues in human FLASH and Lsm11 that are involved in the interaction between these two proteins. We also demonstrate that mutations in the region of FLASH located between amino acids 50 and 99 do not affect binding of Lsm11. Interestingly, these mutations convert FLASH into an inhibitory protein that reduces in vitro processing efficiency of highly active nuclear extracts. Our results suggest that this region in FLASH in conjunction with Lsm11 is involved in recruiting a yet-unknown processing factor(s) to histone pre-mRNA. Following endonucleolytic cleavage of histone pre-mRNA, the downstream cleavage product (DCP) is degraded by the 5′–3′ exonuclease activity of CPSF-73, which also depends on Lsm11. Strikingly, while cleavage of histone pre-mRNA is stimulated by FLASH and inhibited by both dominant negative mutants of FLASH and anti-FLASH antibodies, the 5′–3′ degradation of the DCP is not affected. Thus, the recruitment of FLASH to the processing complex plays a critical role in activating the endonuclease mode of CPSF-73 but is dispensable for its 5′–3′ exonuclease activity. These results suggest that CPSF-73, the catalytic component in both reactions, can be recruited to histone pre-mRNA largely in a manner independent of FLASH, possibly by a separate domain in Lsm11.
Author Lalitha Kunduru
Bing Xu
Ivan Sabath
Zbigniew Dominski
William F. Marzluff
Brandon D. Burch
Xiao-cui Yang
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Snippet Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley...
3′-end cleavage of histone pre-mRNAs is catalyzed by CPSF-73 and requires the interaction of two U7 snRNP-associated proteins, FLASH and Lsm11. Here, by using...
3'-end cleavage of histone pre-mRNAs is catalyzed by CPSF-73 and requires the interaction of two U7 snRNP-associated proteins, FLASH and Lsm11. Here, by using...
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SubjectTerms Amino Acid Sequence
Apoptosis Regulatory Proteins - chemistry
Apoptosis Regulatory Proteins - metabolism
Base Sequence
Binding Sites
Calcium-Binding Proteins - chemistry
Calcium-Binding Proteins - metabolism
DNA Mutational Analysis
Endonucleases - metabolism
Exonucleases - metabolism
Histones - genetics
Histones - metabolism
Humans
Models, Biological
Molecular Sequence Data
Protein Binding
Protein Interaction Mapping
Ribonucleoprotein, U7 Small Nuclear - metabolism
RNA Precursors - metabolism
RNA Processing, Post-Transcriptional
RNA-Binding Proteins - metabolism
Title FLASH Is Required for the Endonucleolytic Cleavage of Histone Pre-mRNAs but Is Dispensable for the 5′ Exonucleolytic Degradation of the Downstream Cleavage Product
URI http://mcb.asm.org/content/31/7/1492.abstract
https://www.tandfonline.com/doi/abs/10.1128/MCB.00979-10
https://www.ncbi.nlm.nih.gov/pubmed/21245389
https://search.proquest.com/docview/1028075016
https://pubmed.ncbi.nlm.nih.gov/PMC3135297
Volume 31
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