Nucleic Acids Research, Vol 26, Issue 16 3707-3716, Copyright © 1998 by Oxford University Press
AM Page, K Davis, C Molineux, RD Kolodner and AW Johnson
Exoribonuclease I from yeast is a 175 kDa protein that is responsible for
the majority of cytoplasmic mRNA degradation. Alignment of the Xrn1p
sequence with homologs from yeast as well as from higher eukaryotes
suggests that the protein is composed of several domains: two acidic
N-terminal domains which likely contain the exonuclease, a basic middle
domainand a basic C-terminal domain. Deletion analysisdemonstrated that the
C-terminus is dispensable for most in vivo and in vitro functions but
confers a dominant negative growth inhibition when expressed at high
levels. This growth inhibition is not due to the exonuclease function of
the protein. To identify specific residues responsible for in vivo
function, a screen was carried out for non-complementing missense
mutations. Fourteen single point mutations were identified that altered
highly conserved amino acids within the first N-terminal domain of Xrn1p.
All of the mutations reduced exonuclease activity measured in vivo and in
vitro using affinity- purified proteins. The mutants fell into two
phenotypic classes, those that reduced or abolished exonuclease activity
without qualitatively changing the products of RNA degradation and those
that gave rise to novel degradation intermediates on certain RNAs.
ARTICLES
Mutational analysis of exoribonuclease I from Saccharomyces cerevisiae
Department of Microbiology and the Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712-1095, USA.
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