Effects of antibody to 5 S-RNA-binding protein on protein synthesis in Artemia salina ribosomes.
The effects of an affinity-purified polyclonal antibody to Artemia salina ribosomal protein L5 on protein synthesis in vitro were examined. The antibody interacted with 60 S subunits more strongly than with 80 S ribosomes, and inhibited reassociation of ribosomal subunits to some extent at 5 mM-Mg2+ but not at 10 mM. Polyphenylalanine synthesis in vitro at 10 mM-Mg2+ was significantly inhibited, especially when the antibody was first preincubated with 60 S subunits prior to the assay. The incorporation of amino acid directed by globin mRNA was inhibited only when the preincubation with 60 S subunits was carried out. On the other hand, no effect was detected on elongation factor 2- and 60 S subunit-dependent uncoupled GTPase activity. These results suggest that L5 is probably located at or near the subunit interface and may play an important role in protein synthesis.
Kenmochi
N
N
Facility for Comparative Medicine, Niigata University School of Medicine, Japan.
Takahashi
Y
Y
Sato
N L
NL
D000818:Animals; D000906:Antibodies / Q000502:physiology*; D001156:Artemia; D002352:Carrier Proteins / Q000276:immunology*; D012335:RNA, Ribosomal / Q000378:metabolism*; D012341:RNA, Ribosomal, 5S / Q000378:metabolism*; D016601:RNA-Binding Proteins; D012269:Ribosomal Proteins / Q000096:biosynthesis*
D000906:Antibodies; D002352:Carrier Proteins; D012335:RNA, Ribosomal; D012341:RNA, Ribosomal, 5S; D016601:RNA-Binding Proteins; D012269:Ribosomal Proteins