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MOLECULAR AND CELLULAR BIOLOGY, 0270-7306/98/$04.00 0
 

Summary: MOLECULAR AND CELLULAR BIOLOGY,
0270-7306/98/$04.00 0
Sept. 1998, p. 50005009 Vol. 18, No. 9
Copyright 1998, American Society for Microbiology. All Rights Reserved.
CUS2, a Yeast Homolog of Human Tat-SF1, Rescues Function of
Misfolded U2 through an Unusual RNA Recognition Motif
DONG YAN, RHONDA PERRIMAN, HALLER IGEL, KENNETH J. HOWE, MEGAN NEVILLE,
AND MANUEL ARES, JR.*
Center for the Molecular Biology of RNA, Biology Department, University of California, Santa Cruz,
Santa Cruz, California 95064
Received 6 April 1998/Returned for modification 14 May 1998/Accepted 8 June 1998
A screen for suppressors of a U2 snRNA mutation identified CUS2, an atypical member of the RNA
recognition motif (RRM) family of RNA binding proteins. CUS2 protein is associated with U2 RNA in splicing
extracts and interacts with PRP11, a subunit of the conserved splicing factor SF3a. Absence of CUS2 renders
certain U2 RNA folding mutants lethal, arguing that a normal activity of CUS2 is to help refold U2 into a
structure favorable for its binding to SF3b and SF3a prior to spliceosome assembly. Both CUS2 function in vivo
and the in vitro RNA binding activity of CUS2 are disrupted by mutation of the first RRM, suggesting that
rescue of misfolded U2 involves the direct binding of CUS2. Human Tat-SF1, reported to stimulate Tat-specific,
transactivating region-dependent human immunodeficiency virus transcription in vitro, is structurally similar
to CUS2. Anti-Tat-SF1 antibodies coimmunoprecipitate SF3a66 (SAP62), the human homolog of PRP11,

  

Source: Ares Jr., Manny - Department of Molecular, Cell, and Developmental Biology, University of California at Santa Cruz

 

Collections: Biology and Medicine