DOI: 10.1002/jcb.21418. Yeast N<sup>α</sup>‐terminal acetyltransferases are associated with ribosomes

Yeast Nα‐terminal acetyltransferases are associated with ribosomes

10.1002/jcb.21418

Crossref journal-article

Wiley

Journal of Cellular Biochemistry (311)

Abstract

AbstractN‐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.

Bibliography

Polevoda, B., Brown, S., Cardillo, T. S., Rigby, S., & Sherman, F. (2007). Yeast NÎ±âterminal acetyltransferases are associated with ribosomes. Journal of Cellular Biochemistry, 103(2), 492â508. Portico.

Authors 5

Bogdan Polevoda (first)
Steven Brown (additional)
Thomas S. Cardillo (additional)
Sean Rigby (additional)
Fred Sherman (additional)

References 52 Referenced 93

10.1128/MCB.5.8.1839
10.1128/EC.5.2.368-378.2006
10.3109/10409238509086784
10.1073/pnas.071057198
10.1073/pnas.062048599
10.1128/MCB.23.20.7403-7414.2003
10.1128/MCB.24.23.10300-10312.2004
10.1074/jbc.272.45.28680
10.1038/sj.embor.7400551
10.1016/0014-5793(70)80312-X
10.1016/S0022-5193(75)80105-6
10.1021/bi00657a008
10.1016/0003-9861(81)90127-2
10.1038/nature01047
10.1016/0014-5793(89)81734-X
10.1016/0022-2836(67)90301-4
10.1016/S0022-2836(02)01111-7
10.1002/j.1460-2075.1989.tb03615.x
10.1073/pnas.75.1.94
10.1002/j.1460-2075.1992.tb05267.x
10.1105/tpc.012377
10.1038/247200a0
10.1021/bi00678a009
10.1021/bi00678a010
10.1074/jbc.R000023200
10.1074/jbc.M011440200
10.1016/S0022-2836(02)01269-X
10.1016/S0006-291X(03)01316-0
10.1093/emboj/18.21.6155
10.1074/jbc.M304690200
10.1126/science.1072366
10.1016/S0960-9822(02)00437-2
10.1002/(SICI)1097-0061(19990330)15:5<397::AID-YEA384>3.0.CO;2-U
10.1101/SQB.1966.031.01.040
10.1038/13732
10.1007/PL00012490
10.1002/yea.320111306
10.1016/S0076-6879(02)50954-X
10.1073/pnas.1232343100
10.1093/genetics/156.2.523 / Genetics / Suppressors of mdm20 in yeast identify new alleles of ACT1 and TPM1 predicted to enhance actin‐tropomysin interactions by Singer JM (2000)
10.1074/jbc.C300355200
10.1016/S0006-291X(74)80498-5
10.1016/S0021-9258(19)88697-0 / J Biol Chem / MAK3 encodes an N‐acetyltransferase whose modification of the L‐A gag NH2 terminus is necessary for virus particle assembly by Tercero JC (1992)
10.1128/jb.175.10.3192-3194.1993
10.1016/S0021-9258(17)40314-0 / J Biol Chem / Protein modification enzymes associated with the protein‐synthesizing complex from rabbit reticulocytes. Protein kinase, phosphoprotein phosphatase, and acetyltransferase by Traugh JA (1977)
10.1016/S0076-6879(79)60050-2
10.1016/0076-6879(84)06016-X
10.1074/jbc.M108848200
10.1038/35001009
10.1002/jcb.10161
10.1534/genetics.104.028803
10.1007/s00018-005-5292-z

Dates

Type	When
Created	18 years, 3 months ago (May 31, 2007, 11:25 a.m.)
Deposited	1 year, 10 months ago (Oct. 8, 2023, 2:59 p.m.)
Indexed	3 days, 9 hours ago (Aug. 30, 2025, 12:25 p.m.)
Issued	18 years, 3 months ago (May 31, 2007)
Published	18 years, 3 months ago (May 31, 2007)
Published Online	18 years, 3 months ago (May 31, 2007)
Published Print	17 years, 7 months ago (Feb. 1, 2008)

Funders 0

None

BibTeX

@article{Polevoda_2007, title={Yeast Nα‐terminal acetyltransferases are associated with ribosomes}, volume={103}, ISSN={1097-4644}, url={http://dx.doi.org/10.1002/jcb.21418}, DOI={10.1002/jcb.21418}, number={2}, journal={Journal of Cellular Biochemistry}, publisher={Wiley}, author={Polevoda, Bogdan and Brown, Steven and Cardillo, Thomas S. and Rigby, Sean and Sherman, Fred}, year={2007}, month=may, pages={492–508} }

JSON

{
  "indexed": {
    "date-parts": [
      [
        2025,
        8,
        30
      ]
    ],
    "date-time": "2025-08-30T16:25:26Z",
    "timestamp": 1756571126500
  },
  "reference-count": 52,
  "publisher": "Wiley",
  "issue": "2",
  "license": [
    {
      "start": {
        "date-parts": [
          [
            2007,
            5,
            31
          ]
        ],
        "date-time": "2007-05-31T00:00:00Z",
        "timestamp": 1180569600000
      },
      "content-version": "vor",
      "delay-in-days": 0,
      "URL": "http://onlinelibrary.wiley.com/termsAndConditions#vor"
    }
  ],
  "content-domain": {
    "domain": [],
    "crossmark-restriction": false
  },
  "published-print": {
    "date-parts": [
      [
        2008,
        2
      ]
    ]
  },
  "abstract": "<jats:title>Abstract</jats:title><jats:p>N\u2010terminal acetylation is one of the most common modifications, occurring on the vast majority of eukaryotic proteins. <jats:italic>Saccharomyces cerevisiae</jats:italic> 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\u2010 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\u2010affinity purified NatA sample. Moreover, Ard1p copurifies with Rpl35p\u2010TAP. 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\u2013508, 2008. \u00a9 2007 Wiley\u2010Liss, Inc.</jats:p>",
  "DOI": "10.1002/jcb.21418",
  "type": "journal-article",
  "created": {
    "date-parts": [
      [
        2007,
        5,
        31
      ]
    ],
    "date-time": "2007-05-31T15:25:05Z",
    "timestamp": 1180625105000
  },
  "page": "492-508",
  "source": "Crossref",
  "is-referenced-by-count": 93,
  "title": "Yeast N<sup>\u03b1</sup>\u2010terminal acetyltransferases are associated with ribosomes",
  "prefix": "10.1002",
  "volume": "103",
  "author": [
    {
      "given": "Bogdan",
      "family": "Polevoda",
      "sequence": "first",
      "affiliation": []
    },
    {
      "given": "Steven",
      "family": "Brown",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Thomas S.",
      "family": "Cardillo",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Sean",
      "family": "Rigby",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Fred",
      "family": "Sherman",
      "sequence": "additional",
      "affiliation": []
    }
  ],
  "member": "311",
  "published-online": {
    "date-parts": [
      [
        2007,
        5,
        31
      ]
    ]
  },
  "reference": [
    {
      "key": "e_1_2_6_2_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1128/MCB.5.8.1839"
    },
    {
      "key": "e_1_2_6_3_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1128/EC.5.2.368-378.2006"
    },
    {
      "key": "e_1_2_6_4_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.3109/10409238509086784"
    },
    {
      "key": "e_1_2_6_5_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1073/pnas.071057198"
    },
    {
      "key": "e_1_2_6_6_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1073/pnas.062048599"
    },
    {
      "key": "e_1_2_6_7_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1128/MCB.23.20.7403-7414.2003"
    },
    {
      "key": "e_1_2_6_8_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1128/MCB.24.23.10300-10312.2004"
    },
    {
      "key": "e_1_2_6_9_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1074/jbc.272.45.28680"
    },
    {
      "key": "e_1_2_6_10_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1038/sj.embor.7400551"
    },
    {
      "key": "e_1_2_6_11_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0014-5793(70)80312-X"
    },
    {
      "key": "e_1_2_6_12_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0022-5193(75)80105-6"
    },
    {
      "key": "e_1_2_6_13_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1021/bi00657a008"
    },
    {
      "key": "e_1_2_6_14_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0003-9861(81)90127-2"
    },
    {
      "key": "e_1_2_6_15_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1038/nature01047"
    },
    {
      "key": "e_1_2_6_16_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0014-5793(89)81734-X"
    },
    {
      "key": "e_1_2_6_17_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0022-2836(67)90301-4"
    },
    {
      "key": "e_1_2_6_18_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0022-2836(02)01111-7"
    },
    {
      "key": "e_1_2_6_19_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1002/j.1460-2075.1989.tb03615.x"
    },
    {
      "key": "e_1_2_6_20_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1073/pnas.75.1.94"
    },
    {
      "key": "e_1_2_6_21_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1002/j.1460-2075.1992.tb05267.x"
    },
    {
      "key": "e_1_2_6_22_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1105/tpc.012377"
    },
    {
      "key": "e_1_2_6_23_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1038/247200a0"
    },
    {
      "key": "e_1_2_6_24_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1021/bi00678a009"
    },
    {
      "key": "e_1_2_6_25_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1021/bi00678a010"
    },
    {
      "key": "e_1_2_6_26_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1074/jbc.R000023200"
    },
    {
      "key": "e_1_2_6_27_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1074/jbc.M011440200"
    },
    {
      "key": "e_1_2_6_28_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0022-2836(02)01269-X"
    },
    {
      "key": "e_1_2_6_29_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0006-291X(03)01316-0"
    },
    {
      "key": "e_1_2_6_30_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1093/emboj/18.21.6155"
    },
    {
      "key": "e_1_2_6_31_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1074/jbc.M304690200"
    },
    {
      "key": "e_1_2_6_32_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1126/science.1072366"
    },
    {
      "key": "e_1_2_6_33_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0960-9822(02)00437-2"
    },
    {
      "key": "e_1_2_6_34_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1002/(SICI)1097-0061(19990330)15:5<397::AID-YEA384>3.0.CO;2-U"
    },
    {
      "key": "e_1_2_6_35_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1101/SQB.1966.031.01.040"
    },
    {
      "key": "e_1_2_6_36_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1038/13732"
    },
    {
      "key": "e_1_2_6_37_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1007/PL00012490"
    },
    {
      "key": "e_1_2_6_38_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1002/yea.320111306"
    },
    {
      "key": "e_1_2_6_39_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0076-6879(02)50954-X"
    },
    {
      "key": "e_1_2_6_40_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1073/pnas.1232343100"
    },
    {
      "key": "e_1_2_6_41_1",
      "doi-asserted-by": "crossref",
      "first-page": "523",
      "DOI": "10.1093/genetics/156.2.523",
      "article-title": "Suppressors of mdm20 in yeast identify new alleles of ACT1 and TPM1 predicted to enhance actin\u2010tropomysin interactions",
      "volume": "156",
      "author": "Singer JM",
      "year": "2000",
      "journal-title": "Genetics"
    },
    {
      "key": "e_1_2_6_42_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1074/jbc.C300355200"
    },
    {
      "key": "e_1_2_6_43_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0006-291X(74)80498-5"
    },
    {
      "key": "e_1_2_6_44_1",
      "doi-asserted-by": "crossref",
      "first-page": "20277",
      "DOI": "10.1016/S0021-9258(19)88697-0",
      "article-title": "MAK3 encodes an N\u2010acetyltransferase whose modification of the L\u2010A gag NH2 terminus is necessary for virus particle assembly",
      "volume": "267",
      "author": "Tercero JC",
      "year": "1992",
      "journal-title": "J Biol Chem"
    },
    {
      "key": "e_1_2_6_45_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1128/jb.175.10.3192-3194.1993"
    },
    {
      "key": "e_1_2_6_46_1",
      "doi-asserted-by": "crossref",
      "first-page": "3738",
      "DOI": "10.1016/S0021-9258(17)40314-0",
      "article-title": "Protein modification enzymes associated with the protein\u2010synthesizing complex from rabbit reticulocytes. Protein kinase, phosphoprotein phosphatase, and acetyltransferase",
      "volume": "252",
      "author": "Traugh JA",
      "year": "1977",
      "journal-title": "J Biol Chem"
    },
    {
      "key": "e_1_2_6_47_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0076-6879(79)60050-2"
    },
    {
      "key": "e_1_2_6_48_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0076-6879(84)06016-X"
    },
    {
      "key": "e_1_2_6_49_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1074/jbc.M108848200"
    },
    {
      "key": "e_1_2_6_50_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1038/35001009"
    },
    {
      "key": "e_1_2_6_51_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1002/jcb.10161"
    },
    {
      "key": "e_1_2_6_52_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1534/genetics.104.028803"
    },
    {
      "key": "e_1_2_6_53_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1007/s00018-005-5292-z"
    }
  ],
  "container-title": "Journal of Cellular Biochemistry",
  "original-title": [],
  "language": "en",
  "link": [
    {
      "URL": "https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fjcb.21418",
      "content-type": "unspecified",
      "content-version": "vor",
      "intended-application": "text-mining"
    },
    {
      "URL": "https://onlinelibrary.wiley.com/doi/pdf/10.1002/jcb.21418",
      "content-type": "unspecified",
      "content-version": "vor",
      "intended-application": "similarity-checking"
    }
  ],
  "deposited": {
    "date-parts": [
      [
        2023,
        10,
        8
      ]
    ],
    "date-time": "2023-10-08T18:59:22Z",
    "timestamp": 1696791562000
  },
  "score": 1,
  "resource": {
    "primary": {
      "URL": "https://onlinelibrary.wiley.com/doi/10.1002/jcb.21418"
    }
  },
  "subtitle": [],
  "short-title": [],
  "issued": {
    "date-parts": [
      [
        2007,
        5,
        31
      ]
    ]
  },
  "references-count": 52,
  "journal-issue": {
    "issue": "2",
    "published-print": {
      "date-parts": [
        [
          2008,
          2
        ]
      ]
    }
  },
  "alternative-id": [
    "10.1002/jcb.21418"
  ],
  "URL": "http://dx.doi.org/10.1002/jcb.21418",
  "relation": {},
  "ISSN": [
    "0730-2312",
    "1097-4644"
  ],
  "subject": [],
  "container-title-short": "J of Cellular Biochemistry",
  "published": {
    "date-parts": [
      [
        2007,
        5,
        31
      ]
    ]
  }
}