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MOLECULAR AND CELLULAR BIOLOGY, 0270-7306/00/$04.00 0
 

Summary: MOLECULAR AND CELLULAR BIOLOGY,
0270-7306/00/$04.00 0
Mar. 2000, p. 21762185 Vol. 20, No. 6
Copyright 2000, American Society for Microbiology. All Rights Reserved.
Functional Cus1p Is Found with Hsh155p in a Multiprotein Splicing
Factor Associated with U2 snRNA
MICHELLE HAYNES PAULING,1
DAVID S. MCPHEETERS,2
AND MANUEL ARES, JR.1
*
Department of Biology and the Center for Molecular Biology of RNA, Sinsheimer Laboratories, University of California,
Santa Cruz, Santa Cruz, California 95064,1
and Department of Biochemistry and the Center for RNA Molecular
Biology, Case Western Reserve University, School of Medicine, Cleveland, Ohio 441062
Received 27 July 1999/Returned for modification 9 September 1999/Accepted 17 December 1999
To explore the dynamics of snRNP structure and function, we have studied Cus1p, identified as a suppressor
of U2 snRNA mutations in budding yeast. Cus1p is homologous to human SAP145, a protein present in the 17S
form of the human U2 snRNP. Here, we define the Cus1p amino acids required for function in yeast. The
segment of Cus1p required for binding to Hsh49p, a homolog of human SAP49, is contained within an essential
region of Cus1p. Antibodies against Cus1p coimmunoprecipitate U2 snRNA, as well as Hsh155p, a protein

  

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

 

Collections: Biology and Medicine