Cotranslational Folding of Globin

We reported data indicating that heme attachment to the globin chains may proceed cotranslationally

Anton A. Komar

2002

Scholarcy highlights

  • We reported data indicating that heme attachment to the globin chains may proceed cotranslationally
  • The data obtained indicated cotranslational heme binding to the nascent globin chains and to the cotranslational folding of the globin molecule since heme binding in the case of globin molecules is
  • Full-length ␣-Globin Is Capable of Cotranslational Heme Binding—It was shown earlier that globin molecules are capable of cotranslational binding of heme in a homologous rabbit reticulocyte cell-free system
  • It is well known that the detachment or displacement of heme groups is accompanied by denaturation of hemoglobin, whereas the addition of the heme group to apohemoglobin or apomyoglobin promotes the formation of the native structure of the molecules
  • On the grounds of these data we suggest that heme binding to the nascent globin chains can be used as a test of cotranslational folding of globins
  • The aim of this work is to determine the length of the nascent globin chain on which heme attachment occurs during translation
  • We have demonstrated an efficient cotranslational incorporation ofhemin into nascent globin chains of 140, 100, and 86 amino acid residues

Need more features? Save interactive summary cards to your Scholarcy Library.