title: Molecular cloning of two small GTP-binding proteins from human skeletal muscle.
abstract: Two distinct cDNAs encoding small GTP-binding proteins were isolated from a human fetal skeletal muscle cDNA library. Nucleotide sequence analysis revealed that one clone encodes a protein of 218 amino acids, which shares highest amino acid identities (over 90%) with the members of YPT3 GTP-binding proteins subfamily and was termed H-YPT3; and the second clone encodes a protein of 201 amino acids, which exhibits strongest homology to rab1A, rab1B, and YPT1 at its N-terminus but diverges notably from these rab family members at the C-terminus. The second cDNA may represents a novel member of the small GTP-binding protein family and was designated H-ray. Northern blot analysis shows that both genes are ubiquitously expressed. Using a bacterial expression vector, each clone was overexpressed in Escherichia coli. The two bacterially produced proteins possess GTP-binding activity.
authors: Department of Medicine, Beth Israel Hospital/Harvard Medical School, Boston, MA 02215.
authors: A X
authors: AX
authors: Zhu
authors: Y
authors: Y
authors: Zhao
authors: J S
authors: JS
authors: Flier
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics; D005260:Female; D019204:GTP-Binding Proteins / Q000235:genetics* / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism; D006801:Humans; D066298:In Vitro Techniques; D051379:Mice; D008969:Molecular Sequence Data; D018482:Muscle, Skeletal / Q000378:metabolism*; D011247:Pregnancy; D051381:Rats; D017386:Sequence Homology, Amino Acid; D014018:Tissue Distribution
chemical_list: D018076:DNA, Complementary; D006160:Guanosine Triphosphate; D019204:GTP-Binding Proteins