Differences in α‐amino acetylation of isozymes of yeast alcohol dehydrogenase

Jörnvall, Hans; Fairwell, T; Kratofil, Paul; Wills, Christopher

doi:10.1016/0014-5793(80)80796-4

Cited by 21 publications

(5 citation statements)

References 18 publications

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“…Furthermore, N-terminal acetylation affects the activity of some of the peptides derived from proopiomelanocortin (Smyth and Zakarian, 1980). However, N-terminal acetylation of isozymes I and H of yeast alcohol dehydrogenase did not affect either their stability or activity (Jornvall et al, 1980). Apparently a subset of all proteins is N-terminally acetylated, but only a portion of this subset requires the modification.…”

Section: Introductionmentioning

confidence: 93%

Identification and characterization of genes and mutants for an N-terminal acetyltransferase from yeast.

et al. 1989

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A gene from Saccharomyces cerevisiae has been mapped, cloned, sequenced and shown to encode a catalytic subunit of an N‐terminal acetyltransferase. Regions of this gene, NAT1, and the chloramphenicol acetyltransferase genes of bacteria have limited but significant homology. A nat1 null mutant is viable but exhibits a variety of phenotypes, including reduced acetyltransferase activity, derepression of a silent mating type locus (HML) and failure to enter G0. All these phenotypes are identical to those of a previously characterized mutant, ard1. NAT1 and ARD1 are distinct genes that encode proteins with no obvious similarity. Concomitant overexpression of both NAT1 and ARD1 in yeast causes a 20‐fold increase in acetyltransferase activity in vitro, whereas overexpression of either NAT1 or ARD1 alone does not raise activity over basal levels. A functional iso‐1‐cytochrome c protein, which is N‐terminally acetylated in a NAT1 strain, is not acetylated in an isogenic nat1 mutant. At least 20 other yeast proteins, including histone H2B, are not N‐terminally acetylated in either nat1 or ard1 mutants. These results suggest that NAT1 and ARD1 proteins function together to catalyze the N‐terminal acetylation of a subset of yeast proteins.

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Section: Introductionmentioning

confidence: 93%

Identification and characterization of genes and mutants for an N-terminal acetyltransferase from yeast.

et al. 1989

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“…The exact role of the addition of acetyl groups to the N-termini of proteins is unclear. N-terminal acetylation increases the stability of some proteins (Johnson et al, 1988), but not others (Jornvall et al, 1980). A null mutant in a yeast Nacetyltransferase exhibits a variety of phenotypes, such as failure to enter the Go phase of the cell cycle and derepression of silent mating type loci (Mullen et al, 1989).…”

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confidence: 99%

The putative tumour suppressor Fus-2 is an N-acetyltransferase

2000

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Acetyltransferases are essential enzymes for a wide variety of cellular processes and mutations in acetyltransferase genes have been associated with the development of certain cancers. For this reason, we conducted a computerized sequence homology search for novel acetyltransferases. Here, we show that the putative tumour suppressor protein Fus-2 has homology to the catalytic domain of acetyltransferases. We demonstrate that Fus-2 can acetylate the N-terminus of proteins using a ping-pong mechanism and that it has a speci®city for substrates. Consistent with other N-acetyltransferases, Fus-2 localizes to the cytoplasm, as shown by GFP-tag experiments. Since the Fus-2 gene maps to the chromosomal region 3p21.3, which contains at least one tumour suppressor gene, the N-acetyltransferase functions of Fus-2 may be relevant to its potential role in cancer.

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“…There is evidence, however, that acetylation can be regulated in response to particular growth conditions. Isozymes of yeast alcohol dehydrogenase have been found to exhibit variation in acetylation during different physiological conditions (18). Similarly, analysis of the ratio of L12 (unacetylated form) to L7 (acetylated form) polypeptides in E. coli ribosomal subunits has shown that L12 is the major form present during early stages of growth, but L7 becomes predominant in stationary phase (36).…”

Section: Discussionmentioning

confidence: 99%

Characterization of traX, the F plasmid locus required for acetylation of F-pilin subunits

Maneewannakul

Ippen‐Ihler

1995

J Bacteriol

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Acetylation of F-pilin subunits has previously been shown to depend upon expression of the F plasmid transfer operon gene traX. To assess the requirement for pilin acetylation in conjugative transfer of F, we constructed traX::kan insertion mutations and crossed them onto the transmissible F derivative pOX38. Under standard conditions, the function of traX seemed to be dispensable. Although pilin synthesized by mutant plasmids pOX38-traX482 and pOX38-traX483 was not acetylated, F-pilus production and F-pilus-specific phage infection appeared to be normal and transfer occurred at wild-type frequency. Analysis of labeled products showed that TraX ؉ plasmids expressed two approximately 24-(TraX1) and 22-kDa (TraX2) polypeptides that localized in the cytoplasmic membranes of cells. No product that was similar in size to the product predicted from the traX open reading frame (27.5 kDa) was detected. Therefore, we used site-directed mutagenesis, stop codon linker insertions, and phoA fusion analysis to investigate traX expression. Both TraX1 and TraX2 appeared to be encoded by the traX open reading frame. Insertion of a stop codon linker into the traX C-terminal coding region led to synthesis of two correspondingly truncated products, and fusions to phoA indicated that only the traX reading frame was translated. Expression was also very dependent on the traX M1 start codon; when this was altered, no protein products were observed. However, pilin acetylation activity was still detectable, indicating that some other in-frame start codon(s) can also be used. All sequences that are essential for activity are contained between traX codons 29 and 225. Sequence analysis indicated that traX mRNA is capable of forming a variety of base-paired structures. We suggest that traX expression is translationally controlled and that F-pilin acetylation activity may be regulated by physiological conditions in cells.

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Differences in α‐amino acetylation of isozymes of yeast alcohol dehydrogenase

Cited by 21 publications

References 18 publications

Identification and characterization of genes and mutants for an N-terminal acetyltransferase from yeast.

Identification and characterization of genes and mutants for an N-terminal acetyltransferase from yeast.

The putative tumour suppressor Fus-2 is an N-acetyltransferase

Characterization of traX, the F plasmid locus required for acetylation of F-pilin subunits

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