Kurvet I, Juganson K, Vija H, Sihtmäe M, Blinova I, Syvertsen-Wiig G, Kahru A (2017) Toxicity of Nine (Doped) Rare Earth Metal Oxides and Respective Individual Metals to Aquatic Microorganisms Vibrio fischeri and Tetrahymena thermophila. Materials (Basel, Switzerland) 10(7): PUBMED:28773114
Wang Y, Wang Y, Sheng Y, Huang J, Chen X, Al-Rasheid KAS, Gao S (2017) A comparative study of genome organization and epigenetic mechanisms in model ciliates, with an emphasis on Tetrahymena, Paramecium and Oxytricha. European journal of protistology ( ): PUBMED:28735853
Wang Y, Feigon J (2017) Structural biology of telomerase and its interaction at telomeres. Current opinion in structural biology 47( ):77-87 PUBMED:28732250
Identifiers and Description
Gene Model Identifier
TTHERM_00292170
Standard Name
ERF1 (Eukaryotic Release Factor )
Aliases
PreTt26050 | 26.m00402 | 3688.m00193
Description
Eukaryotic release factor 1; believed to recognize the stop codon of mRNA and terminate translation; gene has 4 introns; deduced protein sequence 57% similar to human eRF1; domain 1 proposed to be the codon recognition site
SUP45 Polypeptide release fact
or (eRF1) in translation termi
nation; mutant form acts as a
recessive omnipotent suppresso
r; methylated by Mtq2p-Trm112p
in ternary complex eRF1-eRF3-
GTP; mutation of methylation s
ite confers resistance to zymo
cin
Ref:16382136: Salas-Marco J, Fan-Minogue H, Kallmeyer AK, Klobutcher LA, Farabaugh PJ, Bedwell DM (2006) Distinct paths to stop codon reassignment by the variant-code organisms Tetrahymena and Euplotes. Molecular and cellular biology 26(2):438-47
Ref:11788716: Inagaki Y, et al. (2002) Convergence and constraint in eukaryotic release factor 1 (eRF1) domain 1: the evolution of stop codon specificity. Nucleic Acids Res 30(2):532-44
Ref:12084909: Ito K, Frolova L, Seit-Nebi A, Karamyshev A, Kisselev L, Nakamura Y (2002) 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. Proceedings of the National Academy of Sciences of the United States of America 99(13):8494-9
Ref:11163755: Muramatsu T, Heckmann K, Kitanaka C, Kuchino Y (2001) Molecular mechanism of stop codon recognition by eRF1: a wobble hypothesis for peptide anticodons. FEBS letters 488(3):105-9
Ref:11762076: Muramatsu T (2001) [Molecular mechanism of stop codon recognition by eRF1: a wobble hypothesis for peptide anticodons]. Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme 46(15):2163-70
Ref:11231122: Lozupone CA, Knight RD, Landweber LF (2001) The molecular basis of nuclear genetic code change in ciliates. Current biology : CB 11(2):65-74
Ref:11179680: Liang A, Brünen-Nieweler C, Muramatsu T, Kuchino Y, Beier H, Heckmann K (2001) The ciliate Euplotes octocarinatus expresses two polypeptide release factors of the type eRF1. Gene 262(1-2):161-8
Ref:11160924: Inagaki Y, Doolittle WF (2001) Class I release factors in ciliates with variant genetic codes. Nucleic acids research 29(4):921-7
Ref:10648963: Karamyshev AL, Karamysheva ZN, Ito K, Matsufuji S, Nakamura Y (1999) Overexpression and purification of recombinant eRF1 proteins of rabbit and Tetrahymena thermophila. Biochemistry. Biokhimiia 64(12):1391-400
Ref:10471834: Karamyshev AL, Ito K, Nakamura Y (1999) Polypeptide release factor eRF1 from Tetrahymena thermophila: cDNA cloning, purification and complex formation with yeast eRF3. FEBS letters 457(3):483-8
Ref:1160924: Urbanek R, et al. (1975) [Hypophosphataemia as early sign of septicaemia in childhood (author's transl)] Monatsschr Kinderheilkd 123(8):593-7
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