DNA-binding and enzymatic domains of the bifunctional biotin operon repressor (BirA) of Escherichia

Buoncristiani, Martin R.; Howard, Peter K.; Otsuka, Anthony J.

doi:10.1016/0378-1119(86)90189-7

Cited by 69 publications

(43 citation statements)

References 15 publications

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“…BirA ligase plays a key role in cell signaling and chromatin remodeling during biotin biosynthesis in prokaryotes (11,12). Similar mechanisms of gene regulation for HCS have been reported in eukaryotes.…”

Section: Introductionsupporting

confidence: 53%

Prokaryotic BirA ligase biotinylates K4, K9, K18 and K23 in histone H3

Kobza¹,

Sarath²,

Zempleni³

2008

BMB Reports

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Section: Introductionsupporting

confidence: 53%

Prokaryotic BirA ligase biotinylates K4, K9, K18 and K23 in histone H3

Kobza¹,

Sarath²,

Zempleni³

2008

BMB Reports

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“…Mutants that confer a requirement for biotin that is higher than normal are summarized in Table 2 (3,4,21,22). As shown in Figs. 3 Lower and 4a, the sites of most of these mutations are in the vicinity of the bound biotin, although not necessarily in direct contact.…”

Section: Relationship Of the Structure Of The Bira⅐biotin Complex To mentioning

confidence: 99%

Corepressor-induced organization and assembly of the biotin repressor: A model for allosteric activation of a transcriptional regulator

Weaver

Kwon

Beckett

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

105

138

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The Escherichia coli biotin repressor binds to the biotin operator to repress transcription of the biotin biosynthetic operon. In this work, a structure determined by x-ray crystallography of a complex of the repressor bound to biotin, which also functions as an activator of DNA binding by the biotin repressor (BirA), is described. In contrast to the monomeric aporepressor, the complex is dimeric with an interface composed in part of an extended ␤-sheet. Model building, coupled with biochemical data, suggests that this is the dimeric form of BirA that binds DNA. Segments of three surface loops that are disordered in the aporepressor structure are located in the interface region of the dimer and exhibit greater order than was observed in the aporepressor structure. The results suggest that the corepressor of BirA causes a disorder-to-order transition that is a prerequisite to repressor dimerization and DNA binding.

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“…Such a bifunctional nature (BPL/BirA) is also true for Bacillus subtilis BPL (7). (7,11). Figure 3C shows that these residues as well as several other residues of E. coli and B. subtilis BPLs are conserved in other putative group II enzymes.…”

Section: Synthesis Of Biotin and A Biotinylated Proteinmentioning

confidence: 95%

Oxaloacetate Synthesis in the Methanarchaeon Methanosarcina barkeri : Pyruvate Carboxylase Genes and a Putative Escherichia coli -Type Bifunctional Biotin Protein Ligase Gene ( bpl/birA ) Exhibit a Unique Organization

et al. 2001

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Evidence is presented that, in Methanosarcina barkeri oxaloacetate synthesis, an essential and major CO 2 fixation reaction is catalyzed by an apparent ␣ 4 ␤ 4 -type acetyl coenzyme A-independent pyruvate carboxylase (PYC), composed of 64.2-kDa biotinylated and 52.9-kDa ATP-binding subunits. The purified enzyme was most active at 70°C, insensitive to aspartate and glutamate, mildly inhibited by ␣-ketoglutarate, and severely inhibited by ATP, ADP, and excess Mg 2؉ . It showed negative cooperativity towards bicarbonate at 70°C but not at 37°C. The organism expressed holo-PYC without an external supply of biotin and, thus, synthesized biotin. pycA, pycB, and a putative bpl gene formed a novel operon-like arrangement. Unlike other archaeal homologs, the putative biotin protein ligases (BPLs) of M. barkeri and the closely related euryarchaeon Archaeoglobus fulgidus appeared to be of the Escherichia coli-type (bifunctional, with two activities: BirA or a repressor of the biotin operon and BPL). We found the element Tyr(Phe)ProX 5 Phe(Tyr) to be fully conserved in biotindependent enzymes; it might function as the hinge for their "swinging arms."The oxaloacetate (OAA) synthesis step is an essential physiological component and a major CO 2 fixation site in a methanarchaeon (38), for it primes therein an incomplete tricarboxylic acid cycle reaction sequence that generates intermediates for the synthesis of amino acids (via OAA, ␣-ketoglutarate [␣-KG], and succinate) and tetrapyrroles (via ␣-KG) (38). Methanococcus jannaschii and Methanococcus maripaludis use a pyruvate carboxylase (PYC) for OAA synthesis (28, 37). Methanobacterium thermoautotrophicum possesses two OAA-generating enzymes: PYC and phosphoenolpyruvate carboxylase (PPC) (18,22,31). The PYC and PPC reactions take the following forms:The avenue for OAA biosynthesis in Methanosarcina species is unknown. Weimer and Zeikus (42) showed that Methanosarcina barkeri is devoid of PPC activity. We describe below PYC as an OAA-synthesizing activity in M. barkeri and present a biochemical and molecular genetic characterization of the enzyme. (Fig. 1A). Hence, the organism was capable of synthesizing biotin and of biotinylating a candidate polypeptide without any external source of biotin. The intense band at ϳ65 kDa was typical of the biotin-carrying subunit (PYCB) of an arcaheal PYC (28, 31). Thus, we purified and characterized the corresponding protein. As shown below, it possessed PYC activity and the above-mentioned avidinreacting ϳ65-kDa band indeed corresponded to the PYCB subunit of the enzyme (Fig. 1B and C). For the cells grown with a supply of biotin, the relative intensity of the ϳ65-kDa band increased. Thus, M. barkeri exhibited a less stringent version of the control on PYC synthesis seen in Methanobacterium thermoautotrophicum (31); the latter requires exogenously supplied biotin to express holo-PYC (31), although it makes biotin (33), and a similar phenomenon exists in several bacteria (reviewed in reference 31). Whether other bands in the blot (Fig. 1A) r...

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DNA-binding and enzymatic domains of the bifunctional biotin operon repressor (BirA) of Escherichia

Cited by 69 publications

References 15 publications

Prokaryotic BirA ligase biotinylates K4, K9, K18 and K23 in histone H3

Prokaryotic BirA ligase biotinylates K4, K9, K18 and K23 in histone H3

Corepressor-induced organization and assembly of the biotin repressor: A model for allosteric activation of a transcriptional regulator

Oxaloacetate Synthesis in the Methanarchaeon Methanosarcina barkeri : Pyruvate Carboxylase Genes and a Putative Escherichia coli -Type Bifunctional Biotin Protein Ligase Gene ( bpl/birA ) Exhibit a Unique Organization

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