Abstract
Initiation factors M(1) + M(2) from reticulocyte ribosomes bind Met-tRNA(F) to rabbit reticulocyte ribosomes containing endogenous hemoglobin mRNA. The initial binding of Met-tRNA(F) appears to be to the small ribosomal subunit. The Met-tRNA(F) is able to participate in what is presumed to be the first peptide bond in the formation of hemoglobin, namely the synthesis of a methionyl-valine dipeptide. The formation of this methionyl-valine dipeptide requires Met-tRNA(F), initiation factors M(1), M(2), and M(3), as well as Val-tRNA and T(1). No synthesis of methionyl-valine dipeptide takes place if Met-tRNA(F) is replaced by Met-tRNA(M), or if initiation factor M(3) is omitted. Thus, Met-tRNA(F) appears to be the initiator tRNA for hemoglobin biosynthesis and M(3), although required for the synthesis of the first peptide bond of hemoglobin, does not appear to be necessary, under the experimental conditions studied, for Met-tRNA(F) binding.
MeSH Terms
Animals
Binding Sites
Centrifugation, Density Gradient
Chromatography, DEAE-Cellulose
Dipeptides/biosynthesis
Electrophoresis
Formates
Hemoglobins/biosynthesis
Magnesium/pharmacology
Methionine/metabolism
Peptide Chain Initiation, Translational
RNA, Transfer/analysis,metabolism
Rabbits
Receptors, Drug
Reticulocytes/analysis,cytology,metabolism
Ribosomes/metabolism
Sulfur Isotopes
Valine/metabolism
Chemicals
Dipeptides
Formates
Hemoglobins
Receptors, Drug
Sulfur Isotopes
RNA, Transfer
Methionine
Valine
Magnesium
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Crystal R G
Shafritz D A
Prichard P M
Anderson W F
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