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Genetics, Vol. 154, 557-571, February 2000, Copyright © 2000

A Yeast Heterogeneous Nuclear Ribonucleoprotein Complex Associated With RNA Polymerase II

Nicholas K. Conrada, Scott M. Wilsonb, Eric J. Steinmetzc, Meera Patturajana, David A. Browc, Maurice S. Swansonb, and Jeffry L. Cordena
a Department of Molecular Biology and Genetics, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205,
b Department of Molecular Genetics and Microbiology and Centers for Gene Therapy and Mammalian Genetics, College of Medicine, University of Florida, Gainsville, Florida 32610
c Department of Biomolecular Chemistry, University of Wisconsin Medical School, Madison, Wisconsin 53706

Corresponding author: Jeffry L. Corden, Department of Molecular Biology and Genetics, The Johns Hopkins University School of Medicine, 725 N. Wolfe St., Baltimore, MD 21205., jcorden{at}jhmi.edu (E-mail)

Communicating editor: F. WINSTON

Recent evidence suggests a role for the carboxyl-terminal domain (CTD) of the largest subunit of RNA polymerase II (pol II) in pre-mRNA processing. The yeast NRD1 gene encodes an essential RNA-binding protein that shares homology with mammalian CTD-binding proteins and is thought to regulate mRNA abundance by binding to a specific cis-acting element. The present work demonstrates genetic and physical interactions among Nrd1p, the pol II CTD, Nab3p, and the CTD kinase CTDK-I. Previous studies have shown that Nrd1p associates with the CTD of pol II in yeast two-hybrid assays via its CTD-interaction domain (CID). We show that nrd1 temperature-sensitive alleles are synthetically lethal with truncation of the CTD to 9 or 10 repeats. Nab3p, a yeast hnRNP, is a high-copy suppressor of some nrd1 temperature-sensitive alleles, interacts with Nrd1p in a yeast two-hybrid assay, and coimmunoprecipitates with Nrd1p. Temperature-sensitive alleles of NAB3 are suppressed by deletion of CTK1, a kinase that has been shown to phosphorylate the CTD and increase elongation efficiency in vitro. This set of genetic and physical interactions suggests a role for yeast RNA-binding proteins in transcriptional regulation.




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