The Bacillus subtilis spo0B stage 0 sporulation operon encodes an essential GTP-binding protein

Trach, K; Hoch, James A.

doi:10.1128/jb.171.3.1362-1371.1989

Cited by 163 publications

(138 citation statements)

References 29 publications

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“…Different monofunctional chorismate mutases are found in prokaryotes, yeast and plants and probably represent the common ancestral mutase (Xia and Jensen, 1992). Prephenate dehydratases are also found as monofunctional enzymes, in B. subtilis ( Trach and Hoch, 1989) and Corynebacterium glutamicum (Follettie and Sinskey, 1986). No correlation could be made between the monofunctional activities of the enzymes and their involvement in primary or secondary metabolism.…”

Section: Discussionmentioning

confidence: 99%

**Identification and analysis of genes from Streptomyces pristinaespiralis encoding enzymes involved in the biosynthesis of the 4‐dimethylamino‐l‐phenylalanine precursor of pristinamycin I**

Blanc¹,

Gil²,

Bamas‐Jacques³

et al. 1997

Molecular Microbiology

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SummaryFour pap genes (papA, papB, papC, papM ) were found by sequencing near to snbA, a Streptomyces pristinaespiralis gene which was previously shown to encode one of the pristinamycin I (PI) synthetases. Analysis of the homologies observed from the deduced amino acid sequences suggested that these four genes could be involved in the biosynthesis of the PI precursor 4-dimethylamino-L-phenylalanine (DMPAPA). This was first verified when disruption of papA in S. pristinaespiralis led to a PI ¹ phenotype, which was reversed by the addition of DMPAPA into the culture medium. Further confirmation was obtained when papM was overexpressed in Escherichia coli and the corresponding protein purified to homogeneity. It catalysed the two successive N-methylation steps of 4-amino-L-phenylalanine leading to DMPAPA via 4-methylamino-L-phenylalanine. These results allowed us to assign a function to each of the four pap genes and to propose a biosynthetic pathway for DMPAPA.

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Section: Discussionmentioning

confidence: 99%

**Identification and analysis of genes from Streptomyces pristinaespiralis encoding enzymes involved in the biosynthesis of the 4‐dimethylamino‐l‐phenylalanine precursor of pristinamycin I**

Blanc¹,

Gil²,

Bamas‐Jacques³

et al. 1997

Molecular Microbiology

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“…Despite the fact that it is a well-conserved and essential protein, mutants in Obg/ CgtA exhibit a wide variety of phenotypes (reviewed in Czyz andWegrzyn, 2005 andBrown, 2005). In B. subtilis, roles in sporulation initiation, DNA replication, stress response and ribosome function have been suggested (Trach and Hoch, 1989;Vidwans et al, 1995;Scott and Haldenwang, 1999). Other roles for Obg homologues in cellular morphogenesis have been reported.…”

Section: Introductionmentioning

confidence: 99%

Chromosome segregation control by Escherichia coli ObgE GTPase

Foti

Persky²,

Ferullo

et al. 2007

Molecular Microbiology

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SummaryEscherichia coli cells depleted of the conserved GTPase, ObgE, show early chromosome-partitioning defects and accumulate replicated chromosomes in which the terminus regions are colocalized. Cells lacking ObgE continue to initiate replication, with a normal ratio of the origin to terminus. Localization of the SeqA DNA binding protein, normally seen as punctate foci, however, was disturbed. Depletion of ObgE also results in cell filamentation, with polyploid DNA content. Depletion of ObgE did not cause lethality, and cells recovered fully after expression of ObgE was restored. We propose a model in which ObgE is required to license chromosome segregation and subsequent cell cycle events.

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“…Functionally, the Obg-like GTPases are poorly characterized. The beststudied member is the essential Obg/CgtA (SpoOB-associated GTP-binding protein) from Bacillus subtilis (11). Obg and its homologues have been implicated to function in cellular processes as diverse as sporulation, stress response, control of DNA replication, and ribosome assembly (for review see 12).…”

mentioning

confidence: 99%

Human OLA1 Defines an ATPase Subfamily in the Obg Family of GTP-binding Proteins

Koller-Eichhorn

Marquardt

Gail

et al. 2007

Journal of Biological Chemistry

100

140

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Purine nucleotide-binding proteins build the large family of P-loop GTPases and related ATPases, which perform essential functions in all kingdoms of life. The Obg family comprises a group of ancient GTPases belonging to the TRAFAC (for translation factors) class and can be subdivided into several distinct protein subfamilies. The founding member of one of these subfamilies is the bacterial P-loop NTPase YchF, which had so far been assumed to act as GTPase. We have biochemically characterized the human homologue of YchF and found that it binds and hydrolyzes ATP more efficiently than GTP. For this reason, we have termed the protein hOLA1, for human Obg-like ATPase 1. Further biochemical characterization of YchF proteins from different species revealed that ATPase activity is a general but previously missed feature of the YchF subfamily of Obg-like GTPases. To explain ATP specificity of hOLA1, we have solved the x-ray structure of hOLA1 bound to the nonhydrolyzable ATP analogue AMPPCP. Our structural data help to explain the altered nucleotide specificity of YchF homologues and identify the Ola1/YchF subfamily of the Obg-related NTPases as an exceptional example of a single protein subfamily, which has evolved altered nucleotide specificity within a distinct protein family of GTPases.

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The Bacillus subtilis spo0B stage 0 sporulation operon encodes an essential GTP-binding protein

Cited by 163 publications

References 29 publications

**Identification and analysis of genes from Streptomyces pristinaespiralis encoding enzymes involved in the biosynthesis of the 4‐dimethylamino‐l‐phenylalanine precursor of pristinamycin I**

**Identification and analysis of genes from Streptomyces pristinaespiralis encoding enzymes involved in the biosynthesis of the 4‐dimethylamino‐l‐phenylalanine precursor of pristinamycin I**

Chromosome segregation control by Escherichia coli ObgE GTPase

Human OLA1 Defines an ATPase Subfamily in the Obg Family of GTP-binding Proteins

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