The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase.

We report the molecular cloning and DNA sequence carboxylase subunits, biotin carboxylase and carboxyltransof the gene encoding the biotin carboxylase subunit of ferase(Albertsand Vagelos, 1972; Polakis et al., 1974).A

S J Li; J E Cronan

2021

Scholarcy highlights

  • We report the molecular cloning and DNA sequence carboxylase subunits, biotin carboxylase and carboxyltransof the gene encoding the biotin carboxylase subunit of ferase(Albertsand Vagelos, 1972; Polakis et al, 1974).A
  • In E. coli acetyl-coA carboxylase and Propionibacterium shermnii transcarboxylase, the covalently bound biotin, bioticnarboxylase, and carboxyltransferase reside in distinct protein subunits, whereas the higher eucaryotic acetyl-coAcarboxylases and yeast pyruvate carboxylase contain all three components in asingle protein chain
  • Amino- In this papewr e report theDNA sequenceof biotin carboxterminal amino acid sequencing of the purified BCCP ylase and show that this gene is cotranscribed with the gene protein confirmed the deduced amino acid sequence encoding the BCCP subunit
  • Since most recent mechanistic indicating thatBCCP is a protein of atypical physical studies of biotin carboxylation have used E. coli biotin carproperties
  • We found that fusion proteins containing the last 84, 87, or 110 amino acids of BCCP were efficiently biotinated, whereas a 5 ~ LIQPIFRLlL~TNL:L:TN~P" NlHYLE ~ ~ LGLQEK
  • The other species reported can be attributed to cleavages within the Pro/Ala sequences located close to theamino terminus. These carboxyl-terminal peptides interact with the biotin carboxylase and carboxyltransferase subunits, but much more weakly than does the intact BCCP protein.a function of the BCCP amino terminus is to tether BCCP to the other acetyl-coA carboxylase subunits, whereas the central Pro/Ala-rich sequence allows the carboxyl-terminal biotinated domain to move between the subunit active sites

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