Cotranslational heme binding to nascent globin chains.
Globin synthesis in cell-free extracts of rabbit reticulocytes was carried out in the presence of 3H-labeled hemin. Sucrose gradient centrifugation analysis revealed [3H]hemin in the polyribosome fraction. The addition of puromycin resulted in the release of both [3H]hemin- and [14C]leucine-labeled polypeptide from the polyribosomes. The data suggest cotranslational folding of the globin molecule on the ribosome and cotranslational heme binding to the nascent globin chain.
Komar
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Department of Molecular Biology, Faculty of Biology, Moscow State University, Russian Federation.
Kommer
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Krasheninnikov
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Spirin
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AS
D000818:Animals; D002474:Cell-Free System; D002499:Centrifugation, Density Gradient; D005914:Globins / Q000737:chemistry / Q000378:metabolism*; D006427:Hemin / Q000378:metabolism*; D007930:Leucine / Q000378:metabolism; D011132:Polyribosomes / Q000378:metabolism; D014176:Protein Biosynthesis; D017510:Protein Folding; D011691:Puromycin / Q000494:pharmacology; D012333:RNA, Messenger / Q000378:metabolism; D011817:Rabbits; D012156:Reticulocytes / Q000378:metabolism; D014316:Tritium
D012333:RNA, Messenger; D014316:Tritium; D011691:Puromycin; D006427:Hemin; D005914:Globins; D007930:Leucine