Isolation and characterization of a Paracentrotus lividus cDNA encoding a stress-inducible chaperonin.
Chaperonins are ubiquitous proteins that facilitate protein folding in an adenosine triphosphate-dependent manner. Here we report the isolation of a sea urchin cDNA (Plhsp60) coding for mitochondrial chaperonin (Cpn60), whose basal expression is further enhanced by heat shock. The described cDNA corresponds to a full-length mRNA encoding a protein of 582 amino acids, the first 32 of which constitute a putative mitochondrial targeting leader sequence. Comparative analysis has demonstrated that this protein is highly conserved in evolution.
Gianguzza
F
F
Dipartimento di Biologia Cellulare e dello Sviluppo A. Monroy, Palermo, Italy.
Ragusa
M A
MA
Roccheri
M C
MC
Di Liegro
I
I
Rinaldi
A M
AM
D000595:Amino Acid Sequence; D000818:Animals; D018834:Chaperonin 60 / Q000235:genetics* / Q000378:metabolism; D018076:DNA, Complementary / Q000235:genetics; D004625:Embryo, Nonmammalian / Q000378:metabolism; D018869:Heat-Shock Response; D008928:Mitochondria / Q000235:genetics; D008969:Molecular Sequence Data; D012333:RNA, Messenger / Q000378:metabolism; D012617:Sea Urchins / Q000235:genetics* / Q000378:metabolism
D018834:Chaperonin 60; D018076:DNA, Complementary; D012333:RNA, Messenger