돼지 Phosphatidylinositol Glycan, Class K (PIGK) 유전자의 동정과 양적형질과의 연관성 분석
Characterization of Phosphatidylinositol Glycan, Class K (PIGK) Gene and Analysis of Association with Quantitative Traits in Pigs
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PIGK(phosphatidylinositol glycan, class K)는 transamidase의 소단위체로서, 이 효소에 의해서 C-말단 신호서열을 제거하고 GPI에 고정시키는 transamidation 과정에서 중요한 역할을 담당한다. 또한 GPI의 구조와 합성은 인슐린의 세포성 역할과 중요한 연관성을 가지고 있다. 결국 PIGK는 포유류의 발생과 여러 특이적인 세포성 기능뿐만 아니라 GPI와 연관된 인슐린의 대사활성에 필수적이다. full-length cDNAs 서열 분석 결과 두 가지 형태의 서열을 확인하였다. 일반적인 형태의 PIGK 전체서열은 1188bp이고 395개의 아미노산으로 구성되어 있다. 또 다른 형태는 alternative splicing에 의해 intron 7번에서 특이하게 63bp의 삽입현상을 보이며, 삽입서열 내부에서 형성되는 종료코돈(TAG)에 의해 번역이 완성되어 전체서열이 1116bp이며 아미노산 서열은 24개가 줄어든 371개로 구성되어 있음을 확인하였다. F2 545두(KNP × Landrace)를 대상으로 exon 6번에서 발견된 missence mutation (T314I)의 PCR-RFLP 분석을 통하여 성장 및 지방관련 형질들과의 연관성 분석을 수행하였다. 그 결과 CT 유전자형이 도체지방에서 TT 유전자형에 대해 고도의 유의차(P<0.01)를 보였다.
Abstract
PIGK(phosphatidylinositol glycan, class K) is a subunit of GPI transamidase that cleaves the signal peptide in proproteins and replaces it with GPI. In addition, the structure and synthesis of GPI are critically involved in some of the cellular actions of insulin. Therefore, PIGK would be essential for mammalian development and many specific cellular functions as well as for metabolic activity of insulin associated with GPI. Two types of full-length cDNAs of porcine PIGK were cloned through RT-PCR and RACE experiments. One is thought to be a normal form(consist of 395 amino acids) and the other is considered as an alternative spliced form(consist of 371 amino acids) which contains additional 63 bps in intron 7. Since a stop codon was contained within the insertion, the spliced form has a shorter coding sequence than that of normal form. A missense mutation (T314I) in exon 6 was detected and used for genotyping to estimate association with the growth and fat deposition traits for 545 F2 animals(Korean native boars×Landrace). From the PCR-RFLP analysis using HpyCH4III, CT genotype showed highly significant relationship(P<0.01) with carcass fat contents.
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