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

Journal Article · Mon Jan 01 04:00:00 EST 2007 · Molecular Cell

DOI:https://doi.org/10.1016/j.molcel.2007.01.034· OSTI ID:930390

Bai, Y; Auperin, T; Chou, C; Chang, G; Manley, J; Tong, L

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.

• Research Organization: Brookhaven National Laboratory (BNL) National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: AC02-98CH10886
• OSTI ID: 930390
• Report Number(s): BNL--81112-2008-JA
• Journal Information: Molecular Cell, Journal Name: Molecular Cell Journal Issue: 6 Vol. 25; ISSN 1097-2765
• Country of Publication: United States
• Language: English

Related Subjects

36 MATERIALS SCIENCE
CLEAVAGE
CRYSTAL STRUCTURE
DIMERIZATION
LIGHT SCATTERING
MESSENGER-RNA
PRECURSOR
PROTEINS
STIMULATION
ULTRACENTRIFUGATION
YEASTS
national synchrotron light source