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제108회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Crystal structures of two archaeal Pelotas reveal inter-domain structural plasticity

2011년 8월 1일 16시 35분 39초
BIO2-5 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
금 11시 : 25분
생명화학 - Structural Biochemistry and Cellular Signaling
저자 및
국민대학교 생명나노화학과, Korea
Dom34 from Saccharomyces cerevisiae is one of the key players in no-go mRNA decay, a surveillance pathway by which an abnormal mRNA stalled during translation is degraded by an endonucleolytic cleavage. Its homologs called Pelota are found in other species. We showed previously that S. cerevisiae Dom34 (domain 1) has an endoribonuclease activity, which suggests its direct catalytic role in no-go decay. Pelota from Thermoplasma acidophilum and Dom34 from S. cerevisiae have been structurally characterized, revealing a tripartite architecture with significantly different overall conformations from each other. To gain further insights into structural plasticity of the Pelota proteins, we have determined the crystal structures of two archaeal Pelotas from Archaeoglobus fulgidus and Sulfolobus solfataricus. Despite the structural similarity of their individual domains to those of T. acidophilum Pelota and S. cerevisiae Dom34, their overall conformations are distinct from those of T. acidophilum Pelota and S. cerevisiae Dom34. Different overall conformations are due to conformational flexibility of the two linker regions between domains 1?2 and between domains 2?3. The observed inter-domain structural plasticity of Pelota proteins suggests that large conformational changes are essential for their functions.