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Title: Crystal Structure of Murine CstF-77: Dimeric Association and Implications for Polyadenylation of mRNA Precursors

Abstract

Cleavage stimulation factor (CstF) is a heterotrimeric protein complex essential for polyadenylation of mRNA precursors. The 77 kDa subunit, CstF-77, is known to mediate interactions with the other two subunits of CstF as well as with other components of the polyadenylation machinery. We report here the crystal structure of the HAT (half a TPR) domain of murine CstF-77, as well as its C-terminal subdomain. Structural and biochemical studies show that the HAT domain consists of two subdomains, HAT-N and HAT-C domains, with drastically different orientations of their helical motifs. The structures reveal a highly elongated dimer, spanning 165 {angstrom}, with the dimerization mediated by the HAT-C domain. Light-scattering studies, yeast two-hybrid assays, and analytical ultracentrifugation measurements confirm this self-association. The mode of dimerization and the relative arrangement of the HAT-N and HAT-C domains are unique to CstF-77. Our data support a role for CstF dimerization in pre-mRNA 3' end processing.

Authors:
; ; ; ; ;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
930390
Report Number(s):
BNL-81112-2008-JA
Journal ID: ISSN 1097-2765; TRN: US200904%%672
DOE Contract Number:  
DE-AC02-98CH10886
Resource Type:
Journal Article
Resource Relation:
Journal Name: Molecular Cell; Journal Volume: 25; Journal Issue: 6
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE; CLEAVAGE; CRYSTAL STRUCTURE; DIMERIZATION; LIGHT SCATTERING; MESSENGER-RNA; PRECURSOR; PROTEINS; STIMULATION; ULTRACENTRIFUGATION; YEASTS; national synchrotron light source

Citation Formats

Bai,Y., Auperin, T., Chou, C., Chang, G., Manley, J., and Tong, L. Crystal Structure of Murine CstF-77: Dimeric Association and Implications for Polyadenylation of mRNA Precursors. United States: N. p., 2007. Web. doi:10.1016/j.molcel.2007.01.034.
Bai,Y., Auperin, T., Chou, C., Chang, G., Manley, J., & Tong, L. Crystal Structure of Murine CstF-77: Dimeric Association and Implications for Polyadenylation of mRNA Precursors. United States. doi:10.1016/j.molcel.2007.01.034.
Bai,Y., Auperin, T., Chou, C., Chang, G., Manley, J., and Tong, L. Mon . "Crystal Structure of Murine CstF-77: Dimeric Association and Implications for Polyadenylation of mRNA Precursors". United States. doi:10.1016/j.molcel.2007.01.034.
@article{osti_930390,
title = {Crystal Structure of Murine CstF-77: Dimeric Association and Implications for Polyadenylation of mRNA Precursors},
author = {Bai,Y. and Auperin, T. and Chou, C. and Chang, G. and Manley, J. and Tong, L.},
abstractNote = {Cleavage stimulation factor (CstF) is a heterotrimeric protein complex essential for polyadenylation of mRNA precursors. The 77 kDa subunit, CstF-77, is known to mediate interactions with the other two subunits of CstF as well as with other components of the polyadenylation machinery. We report here the crystal structure of the HAT (half a TPR) domain of murine CstF-77, as well as its C-terminal subdomain. Structural and biochemical studies show that the HAT domain consists of two subdomains, HAT-N and HAT-C domains, with drastically different orientations of their helical motifs. The structures reveal a highly elongated dimer, spanning 165 {angstrom}, with the dimerization mediated by the HAT-C domain. Light-scattering studies, yeast two-hybrid assays, and analytical ultracentrifugation measurements confirm this self-association. The mode of dimerization and the relative arrangement of the HAT-N and HAT-C domains are unique to CstF-77. Our data support a role for CstF dimerization in pre-mRNA 3' end processing.},
doi = {10.1016/j.molcel.2007.01.034},
journal = {Molecular Cell},
number = 6,
volume = 25,
place = {United States},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}