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Start Over Descriptor "N-Terminal Acetyltransferase B" Journal journal of cellular biochemistry
2 results on '"N-Terminal Acetyltransferase B"'

1. Yeast Nα-terminal acetyltransferases are associated with ribosomes

Author

Fred Sherman, Steven P. Brown, Thomas S. Cardillo, Sean Taylor Rigby, and Bogdan Polevoda

Subjects
Ribosomal Proteins, NatA complex, Saccharomyces cerevisiae Proteins, Arylamine N-Acetyltransferase, Saccharomyces cerevisiae, Amino-Acid N-Acetyltransferase, Biology, Biochemistry, Ribosome, N-Terminal Acetyltransferases, Acetyltransferases, Ribosomal protein, Polysome, Protein Interaction Mapping, N-Terminal Acetyltransferase C, N-Terminal Acetyltransferase B, Molecular Biology, Cell Biology, Ribosomal RNA, biology.organism_classification, Protein Subunits, Polyribosomes, Eukaryotic Ribosome, Ribosomes, Gene Deletion, NAA15, Protein Binding
Abstract

N-terminal acetylation is one of the most common modifications, occurring on the vast majority of eukaryotic proteins. Saccharomyces cerevisiae contains three major NATs, designated NatA, NatB, and NatC, with each having catalytic subunits Ard1p, Nat3p, and Mak3p, respectively. Gautschi et al. (Gautschi et al. [2003] Mol Cell Biol 23: 7403) previously demonstrated with peptide crosslinking experiments that NatA is bound to ribosomes. In our studies, biochemical fractionation in linear sucrose density gradients revealed that all of the NATs are associated with mono- and polyribosome fractions. However only a minor portion of Nat3p colocalized with the polyribosomes. Disruption of the polyribosomes did not cause dissociation of the NATs from ribosomal subparticles. The NAT auxiliary subunits, Nat1p and Mdm20p, apparently are required for efficient binding of the corresponding catalytic subunits to the ribosomes. Deletions of the genes corresponding to auxiliary subunits significantly diminish the protein levels of the catalytic subunits, especially Nat3p, while deletions of the catalytic subunits produced less effect on the stability of Nat1p and Mdm20p. Also two ribosomal proteins, Rpl25p and Rpl35p, were identified in a TAP-affinity purified NatA sample. Moreover, Ard1p copurifies with Rpl35p-TAP. We suggest that these two ribosomal proteins, which are in close proximity to the ribosomal exit tunnel, may play a role in NatA attachment to the ribosome. J. Cell. Biochem. 103: 492–508, 2008. © 2007 Wiley-Liss, Inc.

Published
2008

2. Yeast N(alpha)-terminal acetyltransferases are associated with ribosomes.

Author

Polevoda B, Brown S, Cardillo TS, Rigby S, and Sherman F

Subjects
Acetyltransferases genetics, Acetyltransferases isolation & purification, Amino-Acid N-Acetyltransferase genetics, Amino-Acid N-Acetyltransferase isolation & purification, Arylamine N-Acetyltransferase genetics, Arylamine N-Acetyltransferase isolation & purification, Gene Deletion, N-Terminal Acetyltransferase B, N-Terminal Acetyltransferase C, N-Terminal Acetyltransferases, Polyribosomes chemistry, Polyribosomes metabolism, Protein Binding, Protein Subunits, Ribosomal Proteins isolation & purification, Ribosomal Proteins metabolism, Ribosomes chemistry, Saccharomyces cerevisiae chemistry, Saccharomyces cerevisiae genetics, Saccharomyces cerevisiae Proteins genetics, Saccharomyces cerevisiae Proteins isolation & purification, Acetyltransferases metabolism, Amino-Acid N-Acetyltransferase metabolism, Arylamine N-Acetyltransferase metabolism, Protein Interaction Mapping, Ribosomes metabolism, Saccharomyces cerevisiae metabolism, Saccharomyces cerevisiae Proteins metabolism
Abstract

N-terminal acetylation is one of the most common modifications, occurring on the vast majority of eukaryotic proteins. Saccharomyces cerevisiae contains three major NATs, designated NatA, NatB, and NatC, with each having catalytic subunits Ard1p, Nat3p, and Mak3p, respectively. Gautschi et al. (Gautschi et al. [2003] Mol Cell Biol 23: 7403) previously demonstrated with peptide crosslinking experiments that NatA is bound to ribosomes. In our studies, biochemical fractionation in linear sucrose density gradients revealed that all of the NATs are associated with mono- and polyribosome fractions. However only a minor portion of Nat3p colocalized with the polyribosomes. Disruption of the polyribosomes did not cause dissociation of the NATs from ribosomal subparticles. The NAT auxiliary subunits, Nat1p and Mdm20p, apparently are required for efficient binding of the corresponding catalytic subunits to the ribosomes. Deletions of the genes corresponding to auxiliary subunits significantly diminish the protein levels of the catalytic subunits, especially Nat3p, while deletions of the catalytic subunits produced less effect on the stability of Nat1p and Mdm20p. Also two ribosomal proteins, Rpl25p and Rpl35p, were identified in a TAP-affinity purified NatA sample. Moreover, Ard1p copurifies with Rpl35p-TAP. We suggest that these two ribosomal proteins, which are in close proximity to the ribosomal exit tunnel, may play a role in NatA attachment to the ribosome., ((c) 2007 Wiley-Liss, Inc.)

Published
2008
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