title: Isolation and characterization of a haploid germ cell-specific novel complementary deoxyribonucleic acid; testis-specific homologue of succinyl CoA:3-Oxo acid CoA transferase.
abstract: We have isolated a cDNA clone encoding a mouse haploid germ cell-specific protein from a subtracted cDNA library. Sequence analysis of the cDNA revealed high homology with pig and human heart succinyl CoA:3-oxo acid CoA transferase (EC 2.8.3.5), which is a key enzyme for energy metabolism of ketone bodies. The deduced protein consists of 520 amino acid residues, including glutamate 344, known to be the catalytic residue in the active site of pig heart CoA transferase and the expected mitochondrial targeting sequence enriched with Arg, Leu, and Ser in the N-terminal region. Thus, we termed this gene scot-t (testis-specific succinyl CoA:3-oxo acid CoA transferase). Northern blot analysis, in situ hybridization, and Western blot analysis demonstrated a unique expression pattern of the mRNA with rapid translation exclusively in late spermatids. The scot-t protein was detected first in elongated spermatids at step 8 or 9 as faint signals and gradually accumulated during spermiogenesis. It was also detected in the midpiece of spermatozoa by immunohistochemistry. The results suggest that the scot-t protein plays important roles in the energy metabolism of spermatozoa.
authors.affiliation: Department of Science for Laboratory Animal Experimentation, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan.
authors.forename: M
authors.initials: M
authors.lastname: Koga
authors.forename: H
authors.initials: H
authors.lastname: Tanaka
authors.forename: K
authors.initials: K
authors.lastname: Yomogida
authors.forename: M
authors.initials: M
authors.lastname: Nozaki
authors.forename: J
authors.initials: J
authors.lastname: Tsuchida
authors.forename: H
authors.initials: H
authors.lastname: Ohta
authors.forename: Y
authors.initials: Y
authors.lastname: Nakamura
authors.forename: K
authors.initials: K
authors.lastname: Masai
authors.forename: Y
authors.initials: Y
authors.lastname: Yoshimura
authors.forename: M
authors.initials: M
authors.lastname: Yamanaka
authors.forename: N
authors.initials: N
authors.lastname: Iguchi
authors.forename: H
authors.initials: H
authors.lastname: Nojima
authors.forename: K
authors.initials: K
authors.lastname: Matsumiya
authors.forename: A
authors.initials: A
authors.lastname: Okuyama
authors.forename: Y
authors.initials: Y
authors.lastname: Nishimune
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D002458:Cell Fractionation; D003001:Cloning, Molecular; D015256:Coenzyme A-Transferases / Q000096:biosynthesis* / Q000235:genetics; D018076:DNA, Complementary / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D015723:Gene Library; D005854:Germ Cells / Q000201:enzymology / Q000378:metabolism* / Q000648:ultrastructure; D006238:Haploidy; D007150:Immunohistochemistry; D017403:In Situ Hybridization; D008297:Male; D051379:Mice; D008810:Mice, Inbred C57BL; D008969:Molecular Sequence Data; D012313:RNA / Q000032:analysis / Q000235:genetics / Q000302:isolation & purification; D013737:Testis / Q000201:enzymology* / Q000648:ultrastructure
chemical_list: D018076:DNA, Complementary; D012313:RNA; D015256:Coenzyme A-Transferases; C021460:3-ketoacid CoA-transferase