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J. Biol. Chem., Vol. 268, Issue 16, 11910-11916, 06, 1993
TA Garrow, AA Brenner, VM Whitehead, XN Chen, RG Duncan, JR Korenberg and B Shane
Human cDNAs for cytosolic and mitochondrial serine hydroxymethyltransferase
(SHMT) were cloned by functional complementation of an Escherichia coli
glyA mutant with a human cDNA library. The cDNA for the cytosolic enzyme
encodes a 483-residue protein of M(r) 53,020. The cDNA for the
mitochondrial enzyme encodes a mature protein of 474 residues of M(r)
52,400. The deduced protein sequences share a high degree of sequence
identity to each other (63%), and the individual isozymes are highly
homologous to the analogous rabbit liver cytosolic (92% identity) and
mitochondrial (97% identity) SHMT isozymes (Martini, F., Angelaccio, S.,
Pascarella, S., Barra, D., Bossa, F., and Schirch, V. (1987) J. Biol. Chem.
262, 5499-5509; Martini, F., Maras, B., Tanci, P., Angelaccio, S.,
Pascarella, S., Barra, D., Bossa, F., and Schirch, V. (1989) J. Biol. Chem.
264, 8509- 8519). SHMT is a highly conserved protein with the human
isozymes retaining about 43% sequence identity with the E. coli protein.
The human cytosolic and mitochondrial SHMT genes were localized to
chromosome regions 17p11.2 and 12q13, respectively. The high degree of
nucleotide sequence identity between the two isozymes, and the presence of
keratin genes in both chromosomal regions, is consistent with these regions
of chromosome 12 and 17 arising by a duplication event.
Cloning of human cDNAs encoding mitochondrial and cytosolic serine hydroxymethyltransferases and chromosomal localization
Department of Nutritional Sciences, University of California, Berkeley 94720.
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