SAP30: Difference between revisions

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Template:PBB Sin3A-associated protein, 30kDa, also known as SAP30, is a protein which in humans is encoded by the SAP30 gene.^[1]

Function

Histone acetylation plays a key role in the regulation of eukaryotic gene expression. Histone acetylation and deacetylation are catalyzed by multisubunit complexes. The protein encoded by this gene is a component of the histone deacetylase complex, which includes SIN3, SAP18, HDAC1, HDAC2, RbAp46, RbAp48, and other polypeptides. This complex is active in deacetylating core histone octamers, but inactive in deacetylating nucleosomal histones. A pseudogene of this gene is located on chromosome 3.^[1]

Mammals have one paralog of SAP30, named SAP30-like (SAP30L), which shares 70 % sequence identity with SAP30.^[2] SAP30 and SAP30L together constitute a well-conserved SAP30 protein family. Also SAP30L interacts with several components of the Sin3A corepressor complex and induces transcriptional repression via recruitment of Sin3A and histone deacetylases.^[3]

Proteins of the SAP30 family (SAP30 proteins) have a functional nucleolar localization signal and they are able to target Sin3A to the nucleolus.^[3] SAP30 proteins have sequence-independent contact with DNA by their N-terminal zinc-dependent module and their acidic central region contributes to histone and nucleosome interactions. The DNA binding of SAP30 proteins is regulated by the nuclear signalling lipids, phosphoinositides (PI).^[4] SAP30 proteins provide the first example in which the DNA and PIs seem to stand in a mutually antagonizing interrelationship in regard to their interaction with zinc finger proteins and thus exemplifies the molecular mechanism how these lipids can contribute for gene regulation.^[4]^[5].

References

^ ^a ^b "Entrez Gene: SAP30 Sin3A-associated protein, 30kDa".
^ Lindfors K, Viiri KM, Niittynen M, Heinonen TY, Mäki M, Kainulainen H (2003). "TGF-beta induces the expression of SAP30L, a novel nuclear protein". BMC Genomics. 4 (1): 53. doi:10.1186/1471-2164-4-53. PMC 319701. PMID 14680513. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)
^ ^a ^b Viiri KM, Korkeamäki H, Kukkonen MK, Nieminen LK, Lindfors K, Peterson P, Mäki M, Kainulainen H, Lohi O (2006). "SAP30L interacts with members of the Sin3A corepressor complex and targets Sin3A to the nucleolus". Nucleic Acids Res. 34 (11): 3288–98. doi:10.1093/nar/gkl401. PMC 1500868. PMID 16820529.{{cite journal}}: CS1 maint: multiple names: authors list (link)
^ ^a ^b Viiri KM, Jänis J, Siggers T, Heinonen TY, Valjakka J, Bulyk ML, Mäki M, Lohi O (2009). "DNA-binding and -bending activities of SAP30L and SAP30 are mediated by a zinc-dependent module and monophosphoinositides". Mol. Cell. Biol. 29 (2): 342–56. doi:10.1128/MCB.01213-08. PMID 19015240. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
^ http://acta.uta.fi/teos.php?id=11179

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 {{Orphan|date=February 2009}}
 {{PBB|geneid=8819}}
-'''Sin3A-associated protein, 30kDa''', also known as '''SAP30''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SAP30 Sin3A-associated protein, 30kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8819| accessdate = }}</ref>
+'''Sin3A-associated protein, 30kDa''', also known as '''SAP30''', is a [[protein]] which in humans is encoded by the SAP30 [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SAP30 Sin3A-associated protein, 30kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8819| accessdate = }}</ref>
+== Function ==
-<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
-{{PBB_Summary
-| section_title =
-| summary_text = Histone acetylation plays a key role in the regulation of eukaryotic gene expression. Histone acetylation and deacetylation are catalyzed by multisubunit complexes. The protein encoded by this gene is a component of the histone deacetylase complex, which includes SIN3, SAP18, HDAC1, HDAC2, RbAp46, RbAp48, and other polypeptides. This complex is active in deacetylating core histone octamers, but inactive in deacetylating nucleosomal histones. A pseudogene of this gene is located on chromosome 3.<ref name="entrez">{{cite web | title = Entrez Gene: SAP30 Sin3A-associated protein, 30kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8819| accessdate = }}</ref>
-}}
+[[Histone]] [[acetylation]] plays a key role in the regulation of eukaryotic gene expression. Histone acetylation and deacetylation are catalyzed by multisubunit complexes. The protein encoded by this gene is a component of the [[histone deacetylase]] complex, which includes SIN3, SAP18, HDAC1, HDAC2, RbAp46, RbAp48, and other polypeptides. This complex is active in deacetylating core histone octamers, but inactive in deacetylating nucleosomal histones. A pseudogene of this gene is located on chromosome 3.<ref name="entrez">{{cite web | title = Entrez Gene: SAP30 Sin3A-associated protein, 30kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8819| accessdate = }}</ref>
-Mammals have one paralog of SAP30, named SAP30-like ('''SAP30L'''), which shares 70 % sequence identity with SAP30<ref>http://www.biomedcentral.com/1471-2164/4/53</ref>. SAP30 and SAP30L together constitute a well-conserved SAP30 protein family. Also SAP30L interacts with several components of the Sin3A corepressor complex and induces transcriptional repression via recruitment of Sin3A and histone deacetylases<ref>http://nar.oxfordjournals.org/cgi/content/full/34/11/3288</ref>. Proteins of the SAP30 family (SAP30 proteins) have a functional nucleolar localization signal and they are able to target Sin3A to the nucleolus<ref>http://nar.oxfordjournals.org/cgi/content/full/34/11/3288</ref>. SAP30 proteins have sequence-independent contact with DNA by their N-terminal zinc-dependent module and their acidic central region contributes to histone and nucleosome interactions. The DNA binding of SAP30 proteins is regulated by the nuclear signalling lipids, phosphoinositides (PI)<ref>http://www.ncbi.nlm.nih.gov/pubmed/19015240?ordinalpos=4&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum</ref>. SAP30 proteins provide the first example in which the DNA and PIs seem to stand in a mutually antagonizing interrelationship in regard to their interaction with zinc finger proteins and thus exemplifies the molecular mechanism how these lipids can contribute for gene regulation<ref>http://www.ncbi.nlm.nih.gov/pubmed/19015240?ordinalpos=4&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum</ref><ref>http://acta.uta.fi/teos.php?id=11179</ref>.
-==References==
+Mammals have one paralog of SAP30, named SAP30-like ([[SAP30L]]), which shares 70 % sequence identity with SAP30.<ref name="pmid14680513">{{cite journal | author = Lindfors K, Viiri KM, Niittynen M, Heinonen TY, Mäki M, Kainulainen H | title = TGF-beta induces the expression of SAP30L, a novel nuclear protein | journal = BMC Genomics | volume = 4 | issue = 1 | pages = 53 | year = 2003 | month = December | pmid = 14680513 | pmc = 319701 | doi = 10.1186/1471-2164-4-53 | url = | issn = }}</ref> SAP30 and SAP30L together constitute a well-conserved SAP30 protein family. Also SAP30L interacts with several components of the Sin3A corepressor complex and induces transcriptional repression via recruitment of Sin3A and histone deacetylases.<ref name="pmid16820529">{{cite journal | author = Viiri KM, Korkeamäki H, Kukkonen MK, Nieminen LK, Lindfors K, Peterson P, Mäki M, Kainulainen H, Lohi O | title = SAP30L interacts with members of the Sin3A corepressor complex and targets Sin3A to the nucleolus | journal = Nucleic Acids Res. | volume = 34 | issue = 11 | pages = 3288–98 | year = 2006 | pmid = 16820529 | pmc = 1500868 | doi = 10.1093/nar/gkl401 | url = | issn = }}</ref>
+Proteins of the SAP30 family (SAP30 proteins) have a functional nucleolar localization signal and they are able to target Sin3A to the nucleolus.<ref name="pmid16820529"/> SAP30 proteins have sequence-independent contact with DNA by their N-terminal zinc-dependent module and their acidic central region contributes to histone and nucleosome interactions. The DNA binding of SAP30 proteins is regulated by the nuclear signalling lipids, phosphoinositides (PI).<ref name="pmid19015240">{{cite journal | author = Viiri KM, Jänis J, Siggers T, Heinonen TY, Valjakka J, Bulyk ML, Mäki M, Lohi O | title = DNA-binding and -bending activities of SAP30L and SAP30 are mediated by a zinc-dependent module and monophosphoinositides | journal = Mol. Cell. Biol. | volume = 29 | issue = 2 | pages = 342–56 | year = 2009 | month = January | pmid = 19015240 | doi = 10.1128/MCB.01213-08 | url = | issn = }}</ref> SAP30 proteins provide the first example in which the DNA and PIs seem to stand in a mutually antagonizing interrelationship in regard to their interaction with zinc finger proteins and thus exemplifies the molecular mechanism how these lipids can contribute for gene regulation.<ref name="pmid19015240"/><ref>http://acta.uta.fi/teos.php?id=11179</ref>.
+== References ==
 {{reflist}}
-==Further reading==
+== Further reading ==
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