N<sup>α</sup>‐acetyltransferase deficiency alters protein synthesis in <i>Saccharomyces cerevisiae</i>

Lee, Fang‐Jen S.; Lai, Lin; Smith, John A.

doi:10.1016/0014-5793(89)81734-x

Cited by 37 publications

(21 citation statements)

References 20 publications

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“…Approximately one-half of yeast proteins are N-terminally acetylated, with most being NatA substrates (3)(4)(5). We can consider that the lack of N-terminal acetylation diminishes activity or stability to various degrees, from no detectable level to the complete loss of function.…”

Section: Discussionmentioning

confidence: 99%

Nat3p and Mdm20p Are Required for Function of Yeast NatB Nα-terminal Acetyltransferase and of Actin and Tropomyosin

Polevoda

Cardillo

Doyle

et al. 2003

Journal of Biological Chemistry

122

139

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NatB N␣-terminal acetyltransferase of Saccharomyces cerevisiae acts cotranslationally on proteins with MetGlu-or Met-Asp-termini and subclasses of proteins with Met-Asn-and Met-Met-termini. NatB is composed of the interacting Nat3p and Mdm20p subunits, both of which are required for acetyltransferase activity. The phenotypes of nat3-⌬ and mdm20-⌬ mutants are identical or nearly the same and include the following: diminished growth at elevated temperatures and on hyperosmotic and nonfermentable media; diminished mating; defective actin cables formation; abnormal mitochondrial and vacuolar inheritance; inhibition of growth by DNAdamaging agents such as methyl methanesulfonate, bleomycin, camptothecin, and hydroxyurea; and inhibition of growth by the antimitotic drugs benomyl and thiabendazole. The similarity of these phenotypes to the phenotypes of certain act1 and tpm1 mutants suggests that such multiple defects are caused by the lack of acetylation of actin and tropomyosins. However, the lack of acetylation of other unidentified proteins conceivably could cause the same phenotypes. Furthermore, unacetylated actin and certain N-terminally altered actins have comparable defective properties in vitro, particularly actin-activated ATPase activity and sliding velocity.The two cotranslational processes, cleavage of N-terminal methionine residues and N-terminal acetylation, are by far the most common modifications, occurring on the vast majority of proteins. Eukaryotic cytosolic proteins initiate with methionine that is cleaved from nascent chains of most proteins. Subsequently, N-terminal acetylation occurs on certain of the proteins, either containing or lacking the methionine residue. This N-terminal acetylation occurs on over one-half of soluble eukaryotic proteins but seldom on prokaryotic proteins (1-3).N-terminal acetylation of proteins is catalyzed by N-terminal acetyltransferases (NATs) 1 that transfer acetyl groups from acetyl-CoA to termini of ␣-amino groups. We have established that Saccharomyces cerevisiae contains three major NATs, NatA, NatB, and NatC, with catalytic subunits Ard1p, Nat3p, and Mak3p, respectively, and that each is required for acetylating different groups of proteins (4, 5). As summarized previously (4, 5), subclasses of proteins with Ser-, Ala-, Gly-, or Thr-termini are acetylated by NatA; proteins with Met-Glu-or Met-Asp-termini and subclasses of proteins with Met-Asn-and Met-Met-termini are acetylated by NatB; and subclasses of proteins with Met-Ile, Met-Leu-, Met-Trp-, or Met-Phe-termini are acetylated by NatC. In addition, a special subclass of NatA substrates with Ser-Glu-, Ser-Asp-, Ala-Glu-, or Gly-Glu-termini, designated NatAЈ, are only partially acetylated in nat3-⌬ or mak3-⌬ mutants (6).In regard to the present study, special emphasis should be made of the NatB substrates, some of which were previously identified by using two-dimensional gel electrophoresis of proteins from normal and nat3-⌬ strains, including the following: actin (Act1p); the small subunit of ribonucleotide...

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Section: Discussionmentioning

confidence: 99%

Nat3p and Mdm20p Are Required for Function of Yeast NatB Nα-terminal Acetyltransferase and of Actin and Tropomyosin

Polevoda

Cardillo

Doyle

et al. 2003

Journal of Biological Chemistry

122

139

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“…The complexity of acetylated termini is reflected in the existence of multiple NATs, each acting on different groups of N termini. In Saccharomyces cerevisiae , three NATs are known: NatA (Lee et al, 1989), NatB , and NatC (Tercero et al, , 1993. NatA contains Nat1p and the catalytic subunit Ard1p (Mullen et al, 1989).…”

Section: Introductionmentioning

confidence: 99%

Cytoplasmic N-Terminal Protein Acetylation Is Required for Efficient Photosynthesis in Arabidopsis[W]

et al. 2003

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The Arabidopsis atmak3-1 mutant was identified on the basis of a decreased effective quantum yield of photosystem II. In atmak3-1 , the synthesis of the plastome-encoded photosystem II core proteins D1 and CP47 is affected, resulting in a decrease in the abundance of thylakoid multiprotein complexes. DNA array-based mRNA analysis indicated that extraplastid functions also are altered. The mutation responsible was localized to AtMAK3 , which encodes a homolog of the yeast protein

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“…In yeast, approximately 40% of the proteins are predicted to have an N-terminal acetyl group, while the corresponding figure for mammalian proteins is almost 90% (16,19,23). Prokaryotic proteins are rarely acetylated (4,32).…”

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confidence: 99%

Physiological Importance and Identification of Novel Targets for the N-Terminal Acetyltransferase NatB

Caesar¹,

Warringer²,

Blomberg³

2006

Eukaryot Cell

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The N-terminal acetyltransferase NatB in Saccharomyces cerevisiae consists of the catalytic subunit Nat3p and the associated subunit Mdm20p. We here extend our present knowledge about the physiological role of NatB by a combined proteomics and phenomics approach. We found that strains deleted for either NAT3 or MDM20 displayed different growth rates and morphologies in specific stress conditions, demonstrating that the two NatB subunits have partly individual functions. Earlier reported phenotypes of the nat3⌬ strain have been associated with altered functionality of actin cables. However, we found that point mutants of tropomyosin that suppress the actin cable defect observed in nat3⌬ only partially restores wild-type growth and morphology, indicating the existence of functionally important acetylations unrelated to actin cable function. Predicted NatB substrates were dramatically overrepresented in a distinct set of biological processes, mainly related to DNA processing and cell cycle progression. Three of these proteins, Cac2p, Pac10p, and Swc7p, were identified as true NatB substrates. To identify N-terminal acetylations potentially important for protein function, we performed a large-scale comparative phenotypic analysis including nat3⌬ and strains deleted for the putative NatB substrates involved in cell cycle regulation and DNA processing. By this procedure we predicted functional importance of the N-terminal acetylation for 31 proteins.

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N^α‐acetyltransferase deficiency alters protein synthesis in Saccharomyces cerevisiae

Cited by 37 publications

References 20 publications

Nat3p and Mdm20p Are Required for Function of Yeast NatB Nα-terminal Acetyltransferase and of Actin and Tropomyosin

Nat3p and Mdm20p Are Required for Function of Yeast NatB Nα-terminal Acetyltransferase and of Actin and Tropomyosin

Cytoplasmic N-Terminal Protein Acetylation Is Required for Efficient Photosynthesis in Arabidopsis[W]

Physiological Importance and Identification of Novel Targets for the N-Terminal Acetyltransferase NatB

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Nα‐acetyltransferase deficiency alters protein synthesis in Saccharomyces cerevisiae

Cited by 37 publications

References 20 publications

Nat3p and Mdm20p Are Required for Function of Yeast NatB Nα-terminal Acetyltransferase and of Actin and Tropomyosin

Nat3p and Mdm20p Are Required for Function of Yeast NatB Nα-terminal Acetyltransferase and of Actin and Tropomyosin

Cytoplasmic N-Terminal Protein Acetylation Is Required for Efficient Photosynthesis in Arabidopsis[W]

Physiological Importance and Identification of Novel Targets for the N-Terminal Acetyltransferase NatB

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N^α‐acetyltransferase deficiency alters protein synthesis in Saccharomyces cerevisiae