GTP-binding domain: three consensus sequence elements with distinct spacing.

Dever, Thomas E.; Glynias, Manuel J.; Merrick, William C.

doi:10.1073/pnas.84.7.1814

Cited by 567 publications

(377 citation statements)

References 57 publications

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“…A characteristic feature of GBPs is that they lack a tripartite GTP-binding consensus motif: the classical third element of this motif (N/ TXPG) [3] is missing in human [4], mouse [4], rat [5] and chicken [6] GBPs. The physiological role of the GBPs in the interferon response is unknown: mouse strains which fail to express GBP1, but which express other GBP family members, are healthy and do not show enhanced susceptibility to viral and other pathogens [7][8][9].…”

Section: Introductionmentioning

confidence: 99%

GTPase properties of the interferon‐induced human guanylate‐binding protein 2

et al. 1996

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Guanylate-binding proteins (GBPs) were originally described as proteins that are strongly induced by interferons and are capable of binding to agarose-immobilized guanine nucleotides, hGBP1, the first of two members of this protein family in humans, was recently shown to represent a novel type of GTPase that hydrolyzes GTP predominantly to GMP. We now report that purified recombinant hGBP2 also hydrolyzes GTP very efficiently, although GDP rather than GMP was the major reaction product. The biochemical parameters of this reaction were as follows: Krn = 313 lEVI, turnover number = 22 min -1. Both hGBP1 and hGBP2 failed to hydrolyze GDP, however, GDP was an effective inhibitor of the hGBP2-but not the hGBPl-catalyzed GTP hydrolysis reaction. Thus, hGBP1 and hGBP2 have similar biochemical properties, but show pronounced differences in product specificity.

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Section: Introductionmentioning

confidence: 99%

GTPase properties of the interferon‐induced human guanylate‐binding protein 2

et al. 1996

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“…In the amino-terminal region, the RHD3 protein was found to contain two conserved motifs present in GTP-binding proteins (GXXXXGKS and DXXG), with a spacing (42 amino acids) that is typical for these motifs ( Fig. 4; Dever et al 1987). …”

Section: Sequence Analyses and Expression Studies Of The Rhd3 Genementioning

confidence: 99%

The ROOT HAIR DEFECTIVE3 gene encodes an evolutionarily conserved protein with GTP-binding motifs and is required for regulated cell enlargement in Arabidopsis.

Wang¹,

Lockwood²,

Hoeltzel³

et al. 1997

Genes Dev.

152

153

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In plants, morphogenesis is largely determined by the orientation and extent of cell enlargement. To define the molecular mechanisms regulating plant cell enlargement, we have conducted a molecular genetic analysis of the ROOT HAIR DEFECTIVES [RHDS) gene of Arabidopsis thaliana. Mutations affecting the RHD3 gene were found to alter cell size, but not cell number, in tissues throughout the plant. Genetic and physiological analyses suggest that the RHD3 gene is not required for proper cell type specification, and it is likely to act downstream of the hormones auxin and ethylene. The RHD3 gene was cloned by a T-DNA tagging method and confirmed by the molecular complementation of the rhd3 mutant phenotype and by the analyses of six rhdS mutant alleles. Consistent with the global effects of the rhd3 mutations, the RHD3 gene is expressed in all major plant organs. The deduced RHDS product is a novel 89-kD polypeptide with putative GTP-binding motifs near the amino terminus. i?iiD3-like genes were identified from a protozoan {Entamoeba histolytica), a fungus {Saccharomyces cerevisiae), and another plant species {Oryza sativa), with the sequence identity including the putative GTP-binding motifs. These results imply that the RHDS protein is a member of a new class of GTP-binding proteins that is widespread in eukaryotes and required for regulated cell enlargement.

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“…We identified a GTP-binding site in the amino-terminal half of BR816 NodQl (GxxxxGK, DxxG and NKxD; Dever et al, 1987) while in the carboxy-terminal region of NodQl we localized an ATP-binding motif (GxxxxGK) and a PAPS motif [K(A/G)xxGxxx-(N/E)x(O or 1)FTl (Satishchandran et al, 1992). These consensus sequences have also been reported for NodQ of S. meliloti (Cervantes et al, 1989), R. tropici (FolchMallol et al, 1996;Laeremans et al, 1996), Rhizobium sp.…”

Section: Sequence Determination and Analysis Of Nodplqlmentioning

confidence: 99%

Functional redundancy of genes for sulphate activation enzymes in Rhizobium sp. BR816

et al. 1997

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The broad-host-range, heat-tolerant Rhizobium strain BR816 produces sulphated Nod metabolites. Two ORFs highly homologous to the Sinorhizo&ium meliloti nodPQ genes were isolated and sequenced. It was found that Rhizo&ium sp. BR816 contained two copies of these genes; one copy was localized on the symbiotic plasmid, the other on the megaplasmid. Both nodP genes were interrupted by insertion of antibiotic resistance cassettes, thus constructing a double nodPlP2 mutant strain. However, no detectable differences in Nod factor TLC profile from this mutant were observed as compared to the wild-type strain. Additionally, plant inoculation experiments did not reveal differences between the mutant strain and the wild-type. It is proposed that a third, functionally homologous locus complements mutations in the Nod factor sulphation genes. Southern blot analysis suggested that this locus contains genes necessary for the sulphation of amino acids.

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GTP-binding domain: three consensus sequence elements with distinct spacing.

Cited by 567 publications

References 57 publications

GTPase properties of the interferon‐induced human guanylate‐binding protein 2

GTPase properties of the interferon‐induced human guanylate‐binding protein 2

The ROOT HAIR DEFECTIVE3 gene encodes an evolutionarily conserved protein with GTP-binding motifs and is required for regulated cell enlargement in Arabidopsis.

Functional redundancy of genes for sulphate activation enzymes in Rhizobium sp. BR816

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