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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 |