Analysis of a clpA-like gene from Arabidopsis thaliana

• Main Authors: Tsai, Cheng-Kun, 蔡丞坤
• Other Authors: Lin Tasi-Yun
• Format: Others
• Language: zh-TW
• Published: 1997
• Online Access: http://ndltd.ncl.edu.tw/handle/63859434533894554417

碩士 === 國立清華大學 === 生命科學系 === 85 === Several Hsps may function as molecular chaperones and some Hsps may promote degradation of heat-damaged proteins during heat stress.Caseinolytic protease-like (Clp-like) proteins comprise a hightly conserved protein family, members of which have been identified in all organisms.ClpA and ClpB form a complex which is an ATP-dependent protease composed of a dodecameric component ClpP and a hexameric component ClpA.The processive degradation of denatured proteins by ClpP-ClpA complex protects cells to survive in the detrimental environment.Our objective was to study the struture of the Arabidopsis clp-lke gene (AtclpA) and the relationships between its expression and heat stress.In this study, a clpA-like gene was isolated from an Arabidopsis cDNA library using the pea clp cDNA (Pspclp) as a probe.The Arabidopsis clpA-like gene was subcloned into pBluescript II KS+ vector and named AtclpA.AtclpA cDNA is 2244 nucleotides in length consisting of a 1998-nucleotide incomplete open reading frame with a 208-nucleotide 3' untranslated sequence plus a poly(A) tail of 38 nucleotides.The open reading frame of the AtclpA shares 89.3% identity with BnclpA of Brassica napus. Analysis of genomic DNA indicates that AtclpA is present as a low-copy-number gene and may contain at least an intron.High temperature treature (37 degree) did not cause an increase an the level of the AtclpA mRNA.Thesis results provide preliminary information for further study on the expression, struture and function of the AtclpA.