Mutational Analyses of Translation Initiation Factor eIF1A in Saccharomyces cerevisiae

Saccharomyces cerevisiae에서 번역 개시 인자 eIF1A 돌연변이에 대한 분석

  • Kwon, Sung-Hun (Department of Biological Sciences, College of Natural Science, Inha University) ;
  • Kim, Jun-Ho (Department of Biological Sciences, College of Natural Science, Inha University) ;
  • Choi, Bo-Kyung (Department of Biological Sciences, College of Natural Science, Inha University) ;
  • Kim, Na-Yeon (Department of Biological Sciences, College of Natural Science, Inha University) ;
  • Choi, Do-Hee (Department of Biological Sciences, College of Natural Science, Inha University) ;
  • Park, Kyoung-Jun (Department of Biological Sciences, College of Natural Science, Inha University) ;
  • Eoh, Jung-Hyun (Department of Biological Sciences, College of Natural Science, Inha University) ;
  • Bae, Sung-Ho (Department of Biological Sciences, College of Natural Science, Inha University)
  • 권성훈 (인하대학교 자연과학대학 생명과학과) ;
  • 김준호 (인하대학교 자연과학대학 생명과학과) ;
  • 최보경 (인하대학교 자연과학대학 생명과학과) ;
  • 김나연 (인하대학교 자연과학대학 생명과학과) ;
  • 최도희 (인하대학교 자연과학대학 생명과학과) ;
  • 박경준 (인하대학교 자연과학대학 생명과학과) ;
  • 어정현 (인하대학교 자연과학대학 생명과학과) ;
  • 배성호 (인하대학교 자연과학대학 생명과학과)
  • Received : 2009.08.26
  • Accepted : 2009.09.21
  • Published : 2009.09.30


Translation initiation factor eIF1A performs essential functions in various initiation steps including 43S preinitiation complex formation in eukaryotes, and contains a highly conserved oligonucleotide-binding (OB) fold. In our previous study, we discovered that eIF1A possesses RNA annealing activity and forms a stable complex with double-stranded RNA. In this study, we initiated site-directed mutations in eIF1A to find the active sites for these biochemical activities and to investigate whether they are essential functions for yeast cell growth. A truncated protein, eIF1A($\Delta$T), devoid of both N- and C-terminal domains but containing an intact OB-fold exhibited RNA annealing activity. In contrast, all point mutations in OB-fold domain, except R57D, impaired both RNA annealing and dsRNA binding activities, indicating that the intact OB-fold domain is required for both activities. Viabilities of the mutant yeast cells were not correlated with RNA annealing activity but with the in vivo protein stabilities in the case of R57D and K94D.


Supported by : 한국학술진흥재단


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