| Summary: | 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.
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