Cotranslational heme binding to nascent globin chains

  • A A A Komar
  • , Aigar Kommer
  • , Igor A. Krasheninnikov
  • , Alexander 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. © 1993.
Original languageEnglish
Pages (from-to)261-263
Number of pages3
JournalFEBS Letters
Volume326
Issue number1-3
DOIs
StatePublished - Jan 1 1993

Keywords

  • Attachment
  • Cotranslational folding
  • Heme
  • Hemoglobin
  • Nascent peptide

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