TY - JOUR
T1 - Polypeptide release factor eRF1 from Tetrahymena thermophila
T2 - cDNA cloning, purification and complex formation with yeast eRF3
AU - Karamyshev, Andrew L.
AU - Ito, Koichi
AU - Nakamura, Yoshikazu
N1 - Funding Information:
We thank Dr. Akemi Hanamura for participation in the early part of this study; Dr. Yoshiyuki Kuchino for collaboration and discussion in the early part of Tt-eRF1 gene cloning; Dr. Toshio Uchiumi for purified rat ribosomes; Dr. Masahiro Fujishima for Tetrahymena thermophila strain; Dr. Senya Matsufuji for Tetrahymena cDNA library; Dr. Olivier Jean-Jean for unpublished information; and Dr. Zemfira Karamysheva for helpful participation in the Tt-eRF1 gene cloning and sequencing. This work was supported in part by grants from the Ministry of Education, Science, Sports and Culture, Japan; the Human Frontier Science Program (awarded in 1993 and 1997); and the Basic Research for Innovation Biosciences Program of Bio-oriented Technology Research Advancement Institution (BRAIN). A.L.K. was a postdoctoral fellow of the Japan Society for the Promotion of Science.
PY - 1999/9/3
Y1 - 1999/9/3
N2 - The first cDNA for the translational release factor eRF1 of ciliates was cloned from Tetrahymena thermophila. The coding frame contained one UAG and nine UAA codons that are reassigned for glutamine in Tetrahymena. The deduced protein sequence is 57% identical to human eRF1. The recombinant Tetrahymena eRF1 purified from a yeast expression system was able to bind to yeast eRF3 as do other yeast or mammalian eRF1s as a prerequisite step for protein termination. The recombinant Tetrahymena eRF1, nevertheless, failed to catalyze polypeptide termination in vitro with rat or Artemia ribosomes, at least in part, due to less efficient binding to the heterologous ribosomes. Stop codon specificity and phylogenetic significance of Tetrahymena eRF1 are discussed from the conservative protein feature. Copyright (C) 1999 Federation of European Biochemical Societies.
AB - The first cDNA for the translational release factor eRF1 of ciliates was cloned from Tetrahymena thermophila. The coding frame contained one UAG and nine UAA codons that are reassigned for glutamine in Tetrahymena. The deduced protein sequence is 57% identical to human eRF1. The recombinant Tetrahymena eRF1 purified from a yeast expression system was able to bind to yeast eRF3 as do other yeast or mammalian eRF1s as a prerequisite step for protein termination. The recombinant Tetrahymena eRF1, nevertheless, failed to catalyze polypeptide termination in vitro with rat or Artemia ribosomes, at least in part, due to less efficient binding to the heterologous ribosomes. Stop codon specificity and phylogenetic significance of Tetrahymena eRF1 are discussed from the conservative protein feature. Copyright (C) 1999 Federation of European Biochemical Societies.
KW - Polypeptide release factor
KW - Tetrahymena thermophila
KW - Translation termination
KW - UGA
KW - eRF1-eRF3 complex
UR - http://www.scopus.com/inward/record.url?scp=0032877150&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0032877150&partnerID=8YFLogxK
U2 - 10.1016/S0014-5793(99)01089-3
DO - 10.1016/S0014-5793(99)01089-3
M3 - Article
C2 - 10471834
AN - SCOPUS:0032877150
SN - 0014-5793
VL - 457
SP - 483
EP - 488
JO - FEBS Letters
JF - FEBS Letters
IS - 3
ER -