Valyl-tRNA synthetase from Artemia. Purification and association with elongation factor 1.
Two components of the protein biosynthetic machinery, valyl-transfer RNA synthetase (VRS) and elongation factor 1 (EF-1), have been isolated as a complex from several mammalian tissues. However, yeast VRS, which lacks an amino-terminal extension, does not associated with EF-1. We purified VRS from the brine shrimp Artemia and investigated its interaction with EF-1. Western blotting of crude Artemia extracts revealed the presence of two forms of VRS, differing in size and capacity to associate with EF-1. About 80% of the total VRS corresponds to a polypeptide of 130 kDa which behaves as a monomer upon gel filtration. Only the larger form of 140 kDa coelutes, cosediments and co-immunoprecipitates with the EF-1 alpha 2 beta gamma delta complex. The ratio of the two forms of VRS remains constant throughout early development. The possible origin and mode of expression of the two forms of VRS present in Artemia are discussed.
Brandsma
M
M
Department of Medical Biochemistry, Sylvius Laboratory, University of Leiden, The Netherlands.
Kerjan
P
P
Dijk
J
J
Janssen
G M
GM
Möller
W
W
D000595:Amino Acid Sequence; D000818:Animals; D001156:Artemia / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D003001:Cloning, Molecular; D007120:Immunochemistry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors / Q000302:isolation & purification* / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D014637:Valine-tRNA Ligase / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism
D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors; D014637:Valine-tRNA Ligase