Backbone and sidechain methyl Ile (delta1), Leu and Val resonance assignments of the catalytic domain of the yeast mRNA decapping enzyme, Dcp2

Mandar V Deshmukh; Yuko Oku; John D Gross

doi:10.1007/s12104-007-9023-2

Backbone and sidechain methyl Ile (delta1), Leu and Val resonance assignments of the catalytic domain of the yeast mRNA decapping enzyme, Dcp2

Biomol NMR Assign. 2007 Jul;1(1):17-8. doi: 10.1007/s12104-007-9023-2. Epub 2007 Jul 21.

Authors

Mandar V Deshmukh¹, Yuko Oku, John D Gross

Affiliation

¹ Department Pharmaceutical Chemistry, University of California San Francisco, 600 16th Street, S-512E, Box 2280, San Francisco, CA 94158, USA.

PMID: 19636815
DOI: 10.1007/s12104-007-9023-2

Abstract

Eukaryotic mRNA decapping by Dcp2 is the penultimate step in several mRNA decay pathways. To understand regulation of Dcp2 by ligand interactions, we have assigned the backbone and sidechain methyl Ile (delta1), Leu and Val chemical shifts of the catalytic domain of the S. Cerevisiae enzyme.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Catalytic Domain
Endoribonucleases / chemistry*
Endoribonucleases / genetics
Isoleucine / analogs & derivatives
Isoleucine / chemistry
Leucine / chemistry
Nuclear Magnetic Resonance, Biomolecular
Protein Structure, Tertiary
Recombinant Fusion Proteins / chemistry
Recombinant Fusion Proteins / genetics
Saccharomyces cerevisiae / enzymology
Saccharomyces cerevisiae / genetics
Saccharomyces cerevisiae Proteins / chemistry*
Saccharomyces cerevisiae Proteins / genetics
Valine / chemistry

Substances

Recombinant Fusion Proteins
Saccharomyces cerevisiae Proteins
mRNA decapping enzymes
Isoleucine
DCP2 protein, S cerevisiae
Endoribonucleases
Leucine
Valine