Cotranslational heme binding to nascent globin chains.

A A Komar; A Kommer; I A Krasheninnikov; A S Spirin

doi:10.1016/0014-5793(93)81803-8

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Cotranslational heme binding to nascent globin chains.

A A Komar·A Kommer·I A Krasheninnikov·A S Spirin

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Abstract

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.

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Animals Cell-Free System Centrifugation, Density Gradient Globins Hemin Leucine Polyribosomes Protein Biosynthesis Protein Folding Puromycin RNA, Messenger Rabbits Reticulocytes Tritium Journal Article Research Support, Non-U.S. Gov't

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A A Komar, A Kommer, I A Krasheninnikov, A S Spirin. 1993-07-12. Cotranslational heme binding to nascent globin chains.. https://doi.org/10.1016/0014-5793(93)81803-8

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