Cotranslational heme binding to nascent globin chains

FEBS Letters

Spirin, Alexander S.¹  Krasheninnikov, Igor A.¹  Kommer, Aigar²  Komar, Anton A.¹ 

[1] Department of Molecular Biology, Faculty of Biology, Moscow State University, 119899 Moscow, Russian Federation;Institute of Protein Research, Russian Academy of Sciences, 142292 Pushchino, Moscow Region, Russian Federation

关键词: Hemoglobin;    Heme;    Attachment;    Nascent peptide;    Cotranslational folding;   

DOI  :  10.1016/0014-5793(93)81803-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown