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PMID: 9854021 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

A conserved motif in the yeast nucleolar protein Nop2p contains an essential cysteine residue.

The Biochemical journal ·Vol. 337 ( Pt 1) ·1999-01-01 ·Pages 29-35

King M, Ton D, Redman KL

Abstract

Nop2p is an essential nucleolar protein in Saccharomyces cerevisiae that is involved in large ribosomal subunit assembly. It has substantial homology with human p120, the proliferation-associated nucleolar antigen that is overexpressed in many human cancers. A motif containing an invariant Pro-Cys dipeptide is found in Nop2p, p120 and the bacterial Fmu proteins. A total of nine conserved residues, including Pro423 and Cys424, were individually altered in Nop2p by site-directed mutagenesis. Nop2p function was abolished by conversion of Cys424 into either alanine or serine. All of the other Nop2p mutations tested sustained yeast viability, including glycine replacement of Pro423 and the conversion of a second conserved cysteine into alanine. The crucial role of Cys424 in Nop2p is intriguing, due to the critical roles that cysteine residues adjacent to a proline have in a number of nucleotide-modifying enzymes.

MeSH Terms
Amino Acid Sequence Amino Acid Substitution Base Sequence Conserved Sequence Cysteine/chemistry DNA Primers Methyltransferases Molecular Sequence Data Mutagenesis, Site-Directed Nuclear Proteins/chemistry,genetics,metabolism Saccharomyces cerevisiae/chemistry Saccharomyces cerevisiae Proteins Sequence Homology, Amino Acid
Chemicals
DNA Primers Nuclear Proteins Saccharomyces cerevisiae Proteins Methyltransferases NOP2 protein, S cerevisiae Cysteine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
King M
Department of Biochemistry and Molecular Biology, Indiana University School of Medicine-Fort Wayne, 2101 Coliseum Boulevard East, Fort Wayne, IN 46805, USA.
Ton D
Redman K L
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1999-01-01
Pages
29-35
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1219932
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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