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학술발표회초록보기

초록문의 abstract@kcsnet.or.kr

결제문의 member@kcsnet.or.kr

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  • 09월 12일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제110회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Phylogenetic analysis of protein kinase C isoforms

등록일
2012년 9월 5일 11시 16분 18초
접수번호
1678
발표코드
BIO.P-777 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
10월 17일 (수요일) 16:00~19:00
발표형식
포스터
발표분야
생명화학
저자 및
공동저자
임선영, 소재원
인하대학교 화학과, Korea
In order to study the evolutionary relationship of the PKC isoforms in various species ranging from yeast to human. Here, we searched, identified, and extracted the PKC sequences from at least 19 different species representing different phyla from yeast to human and aligned the PKC catalytic domain sequences of these proteins to create a phylogenetic tree. Our phylogenetic tree of the PKC isoforms of 19 different species clearly showed the grouping of the PKC isoforms into four branches, namely, aPKCs, cPKCs, and two distinct branches of nPKCs. The PKCdelta and PKCtheta formed the one branch and the PKCepsilon and PKCeta formed the other branch in the phylogenetic tree. Furthermore, we found that in the phylogenetic tree of the PKC catalytic domains, the archetypal yeast PKC isoforms are clustered in the aPKC branch, while in the phylogenetic tree of the PKC C1A domains, the yeast PKC isoforms are clustered in the cPKC branch. In addition, comparison of the domain architectures shows that the yeast PKC isoforms are similar to the nPKC isoforms except for the presence of two Hr1 repeats in yeast. These findings led us to predict that the three classes of the PKC isoforms have been evolved independent of each other rather than by divergence from a common ancestral pair. We next modeled the three-dimensional structures of the PKC catalytic domains from these species and aligned them to see the structural similarities between them. We were able to group the PKC isoforms into distinct clusters on the basis of the structural similarities of their catalytic domains. Furthermore, our studies on the evolutionary pattern of the PKC catalytic domain structures showed that the amino acid residues which lie in and around the active site cleft are evolutionarily well conserved.

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