Characterization of Yeast Translation Initiation Factor 1A and Cloning of Its Essential Gene
作者： Chia-Lin Wei , Mami Kainuma , John W. B. Hershey
关键词: Ribosome 、 Saccharomyces cerevisiae 、 Biology 、 Molecular biology 、 TAF4 、 Yeast 、 Peptide sequence 、 Eukaryotic translation initiation factor 4 gamma 、 Biochemistry 、 Protein biosynthesis 、 Eukaryotic translation
摘要: Abstract Translation initiation factor eIF1A is required in vitro for maximal rates of protein synthesis mammalian systems. It functions primarily by dissociating ribosomes and stabilizing 40 S preinitiation complexes. To better elucidate its precise role promoting the translation process, yeast form has been identified Saccharomyces cerevisiae purified to homogenity on basis cross-reaction with antibodies prepared against eIF1A. The apparent mass (22 kDa) resembles that homolog (20 kDa), active stimulating methionyl-puromycin an assay composed components. gene encoding eIF1A, named TIF11, was cloned shown be single copy. TIF11 encodes a comprising 153 amino acids (17.4 kDa); deduced acid sequence exhibits 65% identity human Both contain clusters positive residues at N terminus negative C terminus. Deletion/disruption demonstrates essential cell growth. Expression cDNA rescues growth defect TIF11-disrupted cells, indicating structure/function highly conserved.
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