Cloning and sequence analysis of the human liver rhodanese: comparison with the bovine and chicken enzymes.
The cDNA for the human rhodanese (thiosulfate: cyanide sulfurtransferase, EC 2.8.1.1), a nuclearly encoded protein of the mitochondrial matrix, was isolated from a human fetal liver cDNA library. Nucleotide sequence revealed an open reading frame coding for a polypeptide of 295 amino acids, which presented a 57% and 58% identity with the bovine and avian rhodanese, respectively. The analysis of the 5'-ends of the coding region gave no evidence for the presence of a cleavable signal sequence as found in other mitochondrial proteins. A comparison with two available amino acid sequences (cow and chicken) showed that sequence similarity is not restricted to the alpha-helices and beta-structures motifs which are remarkably superimposable in the two halves of bovine rhodanese, but extends to adjacent regions.
Pallini
R
R
Istituto di Scienze Neurologiche, Fac. Med. Chir., Università di Siena, Italy.
Guazzi
G C
GC
Cannella
C
C
Cacace
M G
MG
D000311:Adrenal Glands / Q000201:enzymology; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002417:Cattle; D002645:Chickens; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics / Q000302:isolation & purification; D004926:Escherichia coli / Q000235:genetics; D015723:Gene Library; D006801:Humans; D008099:Liver / Q000201:enzymology*; D008969:Molecular Sequence Data; D009838:Oligodeoxyribonucleotides; D016366:Open Reading Frames; D012689:Sequence Homology, Nucleic Acid; D013884:Thiosulfate Sulfurtransferase / Q000235:genetics*
D009838:Oligodeoxyribonucleotides; D004247:DNA; D013884:Thiosulfate Sulfurtransferase