Initial dipeptide formation in hemoglobin biosynthesis.

Publication Type Academic Article
Authors Crystal R, Shafritz D, Prichard P, Anderson W
Journal Proc Natl Acad Sci U S A
Volume 68
Issue 8
Pagination 1810-4
Date Published 08/01/1971
ISSN 0027-8424
Keywords Dipeptides, Hemoglobins, RNA, Transfer, Reticulocytes, Ribosomes
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.
DOI 10.1073/pnas.68.8.1810
PubMed ID 5288768
PubMed Central ID PMC389298
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