A minimal peptide substrate in biotin holoenzyme synthetase‐catalyzed biotinylation
The 14‐mer peptide efficiently mimics the biotin acceptor function of the much larger protein domain normally recognized by BirA, and is identified as the minimum required sequence for biotinylation.
Entropic switch regulates myristate exposure in the HIV-1 matrix protein.
- Chun Tang, Erin Loeliger, P. Luncsford, I. Kinde, D. Beckett, M. Summers
- BiologyProceedings of the National Academy of Sciences…
- 13 January 2004
These findings indicate that the HIV-1 myristyl switch is regulated not by mechanically induced conformational changes, as observed for other myristy switches, but instead by entropic modulation of a preexisting equilibrium.
Biotin sensing: universal influence of biotin status on transcription.
- D. Beckett
- Biology, ChemistryAnnual Review of Genetics
- 12 December 2007
The biotin regulatory system of Escherichia coli, the best characterized of the biotin-sensing systems, functions both as the biotinylating enzyme and as a transcription repressor, and the central role of theBiotin protein ligase in each is reviewed.
Function of a conserved sequence motif in biotin holoenzyme synthetases
Results of this characterization indicate that, rather than functioning in ATP binding, this glycine‐rich sequence is required for binding the substrate biotin and the intermediate in the biotinylation reaction,Biotinyl‐5′‐AMP These results are of general significance for understanding structure‐function relationships in biotin holoenzyme synthetases.
Co-repressor induced order and biotin repressor dimerization: a case for divergent followed by convergent evolution.
Corepressor-induced organization and assembly of the biotin repressor: A model for allosteric activation of a transcriptional regulator
- L. Weaver, K. Kwon, D. Beckett, B. Matthews
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 15 May 2001
The results suggest that the corepressor of BirA causes a disorder-to-order transition that is a prerequisite to repressor dimerization and DNA binding.
Competing protein:protein interactions are proposed to control the biological switch of the E coli biotin repressor
The resulting mutually exclusive protein:protein interfaces explain the novel feature of the BirA regulatory system, namely, that transcription of the genes involved in biotin synthesis is not determined by thelevel of biotin, per se, but by the level of unmodified BCCP.
Self-assembly of bacteriophage lambda cI repressor: effects of single-site mutations on the monomer-dimer equilibrium.
Results show that the structural perturbation accompanying single amino acid replacement does not significantly affect the monomer-dimer equilibrium with the exception of that accompanying replacements of serine 228; mutations at that site weaken the protein-protein interactions responsible for self-association.
Roles of operator and non-operator RNA sequences in bacteriophage R17 capsid assembly.