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Interactions of CstF-64, CstF-77, and symplekin: Implications on localisation and function
Cleavage/polyadenylation of mRNAs and 3′ processing of replication-dependent histone transcripts are both mediated by large complexes that share several protein components. Functional studies of these shared proteins are complicated by the cooperative binding of the individual subunits. For CstF-64,...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
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The American Society for Cell Biology
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3016980/ https://www.ncbi.nlm.nih.gov/pubmed/21119002 http://dx.doi.org/10.1091/mbc.E10-06-0543 |
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author | Ruepp, Marc-David Schweingruber, Christoph Kleinschmidt, Nicole Schümperli, Daniel |
author_facet | Ruepp, Marc-David Schweingruber, Christoph Kleinschmidt, Nicole Schümperli, Daniel |
author_sort | Ruepp, Marc-David |
collection | PubMed |
description | Cleavage/polyadenylation of mRNAs and 3′ processing of replication-dependent histone transcripts are both mediated by large complexes that share several protein components. Functional studies of these shared proteins are complicated by the cooperative binding of the individual subunits. For CstF-64, an additional difficulty is that symplekin and CstF-77 bind mutually exclusively to its hinge domain. Here we have identified CstF-64 and symplekin mutants that allowed us to distinguish between these interactions and to elucidate the role of CstF-64 in the two processing reactions. The interaction of CstF-64 with symplekin is limiting for histone RNA 3′ processing but relatively unimportant for cleavage/polyadenylation. In contrast, the nuclear accumulation of CstF-64 depends on its binding to CstF-77 and not to symplekin. Moreover, the CstF-64 paralogue CstF-64Tau can compensate for the loss of CstF-64. As CstF-64Tau has a lower affinity for CstF-77 than CstF-64 and is relatively unstable, it is the minor form. However, it may become up-regulated when the CstF-64 level decreases, which has biological implications for spermatogenesis and probably also for other regulatory events. Thus, the interactions between CstF-64/CstF-64Tau and CstF-77 are important for the maintenance of stoichiometric nuclear levels of the CstF complex components and for their intracellular localization, stability, and function. |
format | Text |
id | pubmed-3016980 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-30169802011-03-16 Interactions of CstF-64, CstF-77, and symplekin: Implications on localisation and function Ruepp, Marc-David Schweingruber, Christoph Kleinschmidt, Nicole Schümperli, Daniel Mol Biol Cell Articles Cleavage/polyadenylation of mRNAs and 3′ processing of replication-dependent histone transcripts are both mediated by large complexes that share several protein components. Functional studies of these shared proteins are complicated by the cooperative binding of the individual subunits. For CstF-64, an additional difficulty is that symplekin and CstF-77 bind mutually exclusively to its hinge domain. Here we have identified CstF-64 and symplekin mutants that allowed us to distinguish between these interactions and to elucidate the role of CstF-64 in the two processing reactions. The interaction of CstF-64 with symplekin is limiting for histone RNA 3′ processing but relatively unimportant for cleavage/polyadenylation. In contrast, the nuclear accumulation of CstF-64 depends on its binding to CstF-77 and not to symplekin. Moreover, the CstF-64 paralogue CstF-64Tau can compensate for the loss of CstF-64. As CstF-64Tau has a lower affinity for CstF-77 than CstF-64 and is relatively unstable, it is the minor form. However, it may become up-regulated when the CstF-64 level decreases, which has biological implications for spermatogenesis and probably also for other regulatory events. Thus, the interactions between CstF-64/CstF-64Tau and CstF-77 are important for the maintenance of stoichiometric nuclear levels of the CstF complex components and for their intracellular localization, stability, and function. The American Society for Cell Biology 2011-01-01 /pmc/articles/PMC3016980/ /pubmed/21119002 http://dx.doi.org/10.1091/mbc.E10-06-0543 Text en © 2011 Ruepp et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,“ “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Ruepp, Marc-David Schweingruber, Christoph Kleinschmidt, Nicole Schümperli, Daniel Interactions of CstF-64, CstF-77, and symplekin: Implications on localisation and function |
title | Interactions of CstF-64, CstF-77, and symplekin: Implications on localisation and function |
title_full | Interactions of CstF-64, CstF-77, and symplekin: Implications on localisation and function |
title_fullStr | Interactions of CstF-64, CstF-77, and symplekin: Implications on localisation and function |
title_full_unstemmed | Interactions of CstF-64, CstF-77, and symplekin: Implications on localisation and function |
title_short | Interactions of CstF-64, CstF-77, and symplekin: Implications on localisation and function |
title_sort | interactions of cstf-64, cstf-77, and symplekin: implications on localisation and function |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3016980/ https://www.ncbi.nlm.nih.gov/pubmed/21119002 http://dx.doi.org/10.1091/mbc.E10-06-0543 |
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