2bze: Difference between revisions

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==Overview==

The yeast Paf1 complex consists of Paf1, Rtf1, Cdc73, Ctr9, and Leo1 and, regulates histone H2B ubiquitination, histone H3 methylation, RNA, polymerase II carboxy-terminal domain (CTD) Ser2 phosphorylation, and RNA, 3' end processing. We provide structural insight into the Paf1 complex, with the NMR structure of the conserved and functionally important Plus3, domain of human Rtf1. A predominantly beta-stranded subdomain displays, structural similarity to Dicer/Argonaute PAZ domains and to Tudor domains., We further demonstrate that the highly basic Rtf1 Plus3 domain can, interact in vitro with single-stranded DNA via residues on the rim of the, beta sheet, reminiscent of siRNA binding by PAZ domains, but did not, detect binding to double-stranded DNA or RNA. We discuss the potential, role of Rtf1 Plus3 ssDNA binding during transcription elongation.

The yeast Paf1 complex consists of Paf1, Rtf1, Cdc73, Ctr9, and Leo1 and regulates histone H2B ubiquitination, histone H3 methylation, RNA polymerase II carboxy-terminal domain (CTD) Ser2 phosphorylation, and RNA 3' end processing. We provide structural insight into the Paf1 complex with the NMR structure of the conserved and functionally important Plus3 domain of human Rtf1. A predominantly beta-stranded subdomain displays structural similarity to Dicer/Argonaute PAZ domains and to Tudor domains. We further demonstrate that the highly basic Rtf1 Plus3 domain can interact in vitro with single-stranded DNA via residues on the rim of the beta sheet, reminiscent of siRNA binding by PAZ domains, but did not detect binding to double-stranded DNA or RNA. We discuss the potential role of Rtf1 Plus3 ssDNA binding during transcription elongation.

==About this Structure==

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==Reference==

Structure and DNA binding of the human ~~rtf1 plus3~~ domain., de Jong RN, Truffault V, Diercks T, Ab E, Daniels MA, Kaptein R, Folkers GE, Structure. 2008 Jan;16(1):149-59. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18184592 18184592]

Structure and DNA binding of the human Rtf1 Plus3 domain., de Jong RN, Truffault V, Diercks T, Ab E, Daniels MA, Kaptein R, Folkers GE, Structure. 2008 Jan;16(1):149-59. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18184592 18184592]

[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Ab, E.]]

[[Category: Daniels, M.A.]]

[[Category: Daniels, M A.]]

[[Category: Diercks, T.]]

[[Category: Folkers, G.E.]]

[[Category: Folkers, G E.]]

[[Category: Jong, R.N.De.]]

[[Category: Jong, R N.De.]]

[[Category: Kaptein, R.]]

[[Category: Spine, Structural.Proteomics.in.Europe.]]

[[Category: Spine, Structural Proteomics in Europe.]]

[[Category: Truffault, V.]]

[[Category: cdc73]]

Line 36:

[[Category: transcription regulation]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-The yeast Paf1 complex consists of Paf1, Rtf1, Cdc73, Ctr9, and Leo1 and, regulates histone H2B ubiquitination, histone H3 methylation, RNA, polymerase II carboxy-terminal domain (CTD) Ser2 phosphorylation, and RNA, 3' end processing. We provide structural insight into the Paf1 complex, with the NMR structure of the conserved and functionally important Plus3, domain of human Rtf1. A predominantly beta-stranded subdomain displays, structural similarity to Dicer/Argonaute PAZ domains and to Tudor domains., We further demonstrate that the highly basic Rtf1 Plus3 domain can, interact in vitro with single-stranded DNA via residues on the rim of the, beta sheet, reminiscent of siRNA binding by PAZ domains, but did not, detect binding to double-stranded DNA or RNA. We discuss the potential, role of Rtf1 Plus3 ssDNA binding during transcription elongation.
+The yeast Paf1 complex consists of Paf1, Rtf1, Cdc73, Ctr9, and Leo1 and regulates histone H2B ubiquitination, histone H3 methylation, RNA polymerase II carboxy-terminal domain (CTD) Ser2 phosphorylation, and RNA 3' end processing. We provide structural insight into the Paf1 complex with the NMR structure of the conserved and functionally important Plus3 domain of human Rtf1. A predominantly beta-stranded subdomain displays structural similarity to Dicer/Argonaute PAZ domains and to Tudor domains. We further demonstrate that the highly basic Rtf1 Plus3 domain can interact in vitro with single-stranded DNA via residues on the rim of the beta sheet, reminiscent of siRNA binding by PAZ domains, but did not detect binding to double-stranded DNA or RNA. We discuss the potential role of Rtf1 Plus3 ssDNA binding during transcription elongation.
 ==About this Structure==
@@ Line 10: / Line 10: @@
 ==Reference==
-Structure and DNA binding of the human rtf1 plus3 domain., de Jong RN, Truffault V, Diercks T, Ab E, Daniels MA, Kaptein R, Folkers GE, Structure. 2008 Jan;16(1):149-59. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18184592 18184592]
+Structure and DNA binding of the human Rtf1 Plus3 domain., de Jong RN, Truffault V, Diercks T, Ab E, Daniels MA, Kaptein R, Folkers GE, Structure. 2008 Jan;16(1):149-59. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18184592 18184592]
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
 [[Category: Ab, E.]]
-[[Category: Daniels, M.A.]]
+[[Category: Daniels, M A.]]
 [[Category: Diercks, T.]]
-[[Category: Folkers, G.E.]]
+[[Category: Folkers, G E.]]
-[[Category: Jong, R.N.De.]]
+[[Category: Jong, R N.De.]]
 [[Category: Kaptein, R.]]
-[[Category: Spine, Structural.Proteomics.in.Europe.]]
+[[Category: Spine, Structural Proteomics in Europe.]]
 [[Category: Truffault, V.]]
 [[Category: cdc73]]
@@ Line 36: / Line 36: @@
 [[Category: transcription regulation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 10:37:42 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:43:14 2008''