The Journal of Nutritional Biochemistry
Volume 16, Issue 7 , Pages 416-418 , July 2005

Targeted and proximity-dependent promiscuous protein biotinylation by a mutant Escherichia coli biotin protein ligase

  • John E. Cronan

      Affiliations

    • Corresponding Author InformationDepartment of Microbiology, University of Illinois, Urbana, IL 61801, USA. Tel.: +1 217 333 7919; fax: +1 217 244 6697.

Received 28 March 2005 ,Revised 28 March 2005 ,Accepted 28 March 2005.

References 

  1. Chapman-Smith A, Cronan JE. The enzymatic biotinylation of proteins: a post-translational modification of exceptional specificity. Trends Biochem Sci. 1999;24:359–363
  2. Choi-Rhee E, Schulman H, Cronan JE. Promiscuous protein biotinylation by Escherichia coli biotin protein ligase. Protein Sci. 2004;13:3043–3050
  3. Kwon K, Beckett D. Function of a conserved sequence motif in biotin holoenzyme synthetases. Protein Sci. 2000;9:1530–1539
  4. Xu Y, Beckett D. Evidence for interdomain interaction in the Escherichia coli repressor of biotin biosynthesis from studies of an N-terminal domain deletion mutant. Biochemistry. 1996;35:1783–1792

☆ This paper was presented at the international symposium “Vitamins as Regulators of Genetic Expression: Biotin as a Model” NAFTA Satellite Meeting to the XXV National Congress of Biochemistry held on December 3–4, 2004, in Ixtapa, Zihuatanejo, Mexico. This meeting was sponsored by Sociedad Mexicana de Bioquimica A.C.; Programa de Doctorado en Ciencias Biomedicas, Universidad Nacional Autonoma de Mexico; Laboratorios Roche–Syntex, Mexico; and Instituto de Investigaciones Biomedicas, Universidad Nacional Autonoma de Mexico.

PII: S0955-2863(05)00090-2

doi: 10.1016/j.jnutbio.2005.03.017

The Journal of Nutritional Biochemistry
Volume 16, Issue 7 , Pages 416-418 , July 2005

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