HemK2 protein, encoded on human chromosome 21, methylates translation termination factor eRF1

被引：67

作者：

Figaro, Sabine ^{[1
]}

Scrima, Nathalie ^{[1
]}

Buckingham, Richard H. ^{[1
]}

Heurgue-Hamard, Valerie ^{[1
]}

机构：

[1] IBPC, CNRS, UPR 9073, F-75005 Paris, France

来源：

FEBS LETTERS | 2008年 / 582卷 / 16期

关键词：

HemK2; methyltransferase; eRF1; N5-methylglutamine; hTrm112; human chromosome 21;

D O I：

10.1016/j.febslet.2008.05.045

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The ubiquitous tripeptide Gly-Gly-Gln in class 1 polypeptide release factors triggers polypeptide release on ribosomes. The Gln residue in both bacterial and yeast release factors is N5-methylated, despite their distinct evolutionary origin. Methylation of eRF1 in yeast is performed by the heterodimeric methyltransferase ( MTase) Mtq2p/Trm112p, and requires eRF3 and GTP. Homologues of yeast Mtq2p and Trm112p are found in man, annotated as an N6-DNA-methyltransferase and of unknown function. Here we show that the human proteins methylate human and yeast eRF1. eRF3. GTP in vitro, and that the MTase catalytic subunit can complement the growth defect of yeast strains deleted for mtq2.

引用

页码：2352 / 2356

页数：5

共 50 条

[41] Human release factor eRF1: structural organisation of the unique functional gene on chromosome 5 and of the three processed pseudogenes
Guenet, L
Toutain, B
Guilleret, I
Chauvel, B
Deaven, LL
Longmire, JL
Le Gall, JY
David, V
Le Treut, A
FEBS LETTERS, 1999, 454 (1-2) : 131 - 136
[42] Exploring contacts of eRF1 with the 3′-terminus of the P site tRNA and mRNA stop signal in the human ribosome at various translation termination steps
Bulygin, Konstantin N.
Graifer, Dmitri M.
Hountondji, Codjo
Frolova, Ludmila Yu.
Karpova, Galina G.
BIOCHIMICA ET BIOPHYSICA ACTA-GENE REGULATORY MECHANISMS, 2017, 1860 (07): : 782 - 793
[43] Eukaryotic translation termination factor gene (ETF1/eRF1) maps at D5S500 in a commonly deleted region of chromosome 5q31 in malignant myeloid diseases
Guenet, L
Henry, C
Toutain, B
Dubourg, C
Le Gall, JY
David, V
Le Treut, A
CYTOGENETICS AND CELL GENETICS, 2000, 88 (1-2): : 82 - 86
[44] Omnipotent decoding potential resides in eukaryotic translation termination factor eRF1 of variant-code organisms and is modulated by the interactions of amino acid sequences within domain 1
Ito, K
Frolova, L
Seit-Nebi, A
Karamyshev, A
Kisselev, L
Nakamura, Y
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (13) : 8494 - 8499
[45] Termination of translation in eukaryotes is mediated by the quaternary eRF1•eRF3•GTP•Mg2+ complex.: The biological roles of eRF3 and prokaryotic RF3 are profoundly distinct
Mitkevich, Vladimir A.
Kononenko, Artem V.
Petrushanko, Irina Yu.
Yanvarev, Dmitry V.
Makarov, Alexander A.
Kisselev, Lev L.
NUCLEIC ACIDS RESEARCH, 2006, 34 (14) : 3947 - 3954
[46] Eukaryotic class I translation termination factor eRF1 - the NMR structure and dynamics of the middle domain involved in triggering ribosome-dependent peptidyl-tRNA hydrolysis
Ivanova, Elena V.
Kolosov, Peter M.
Birdsall, Berry
Kelly, Geoff
Pastore, Annalisa
Kisselev, Lev L.
Polshakov, Vladimir I.
FEBS JOURNAL, 2007, 274 (16) : 4223 - 4237
[47] Conservation of translation termination factor eRF3 in evolution: mouse eRF3m2 but not eRF3m1 could functionally substitute yeast eRF3.
Zemlyanko, O
Le Goff, C
Philippe, M
Zhouravleva, G
YEAST, 2001, 18 : S67 - S67
[48] Human HemK2/KMT9/N6AMT1 is an active protein methyltransferase, but does not act on DNA in vitro, in the presence of Trm112
Clayton B. Woodcock
Dan Yu
Xing Zhang
Xiaodong Cheng
Cell Discovery, 5
[49] Human HemK2/KMT9/N6AMT1 is an active protein methyltransferase, but does not act on DNA in vitro, in the presence of Trm112
Woodcock, Clayton B.
Yu, Dan
Zhang, Xing
Cheng, Xiaodong
CELL DISCOVERY, 2019, 5
[50] Eukaryotic translation termination factor 1 associates with protein phosphatase 2A and targets it to ribosomes
Lechward, K
Zolnierowicz, S
Hemmings, BA
BIOCHEMISTRY-MOSCOW, 1999, 64 (12) : 1373 - 1381

← 1 2 3 4 5 →