NDLI: CDNA cloning of goldfish Hsp27 and its chaperone activity

Content Provider	Springer Nature Link
Author	Kondo, Hidehiro Harano, Ryouhei Watabe, Shugo
Copyright Year	2007
Abstract	A cDNA fragment encoding goldfish Hsp27 was amplified by polymerase chain reaction and its nucleotide sequence was determined. The deduced amino-acid sequence of goldfish Hsp27 showed 58–62% identity to Hsp27 from other vertebrates. Three serine residues reported to be phosphorylated in human Hsp27 were conserved in goldfish Hsp27. The Hsp27 gene was transcribed in goldfish culture cells after temperature shift from 20°C to 40°C, but not from 20°C to 35°C. Recombinant goldfish Hsp27 was examined for its in vitro chaperone activity and compared to those of Hsp30 from the same fish and human recombinant Hsp27. Goldfish Hsp27 and Hsp30 showed a similar activity at 10 μM, which was significantly lower than that of human Hsp27. At 1 and 5 μM concentrations, however, goldfish Hsp27 showed slightly lower activity than goldfish Hsp30, but the activities of both goldfish proteins still remained significantly lower than that of human Hsp27. Meanwhile, goldfish Hsp27 formed oligomer, which was slightly smaller than that of Hsp30. These results suggest that goldfish Hsp27 contributes as a molecular chaperone in association with Hsp30 to compensate for stress resulting from rapid temperature fluctuations.
Starting Page	950
Ending Page	957
Page Count	8
File Format	PDF
ISSN	09199268
Journal	Fisheries Science
Volume Number	73
Issue Number	4
e-ISSN	14442906
Language	English
Publisher	Springer-Verlag
Publisher Date	2007-01-01
Publisher Place	Tokyo
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	chaperone activity culture cell goldfish Hsp27 Hsp30 Fish & Wildlife Biology & Management Freshwater & Marine Ecology Food Science
Content Type	Text
Resource Type	Article
Subject	Aquatic Science

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