نتایج جستجو برای: sinorhizobium meliloti

تعداد نتایج: 2270  

2015
Aaron P McGrath Elise L Laming G Patricia Casas Garcia Marc Kvansakul J Mitchell Guss Jill Trewhella Benoit Calmes Paul V Bernhardt Graeme R Hanson Ulrike Kappler Megan J Maher Michael A Marletta

Interprotein electron transfer underpins the essential processes of life and relies on the formation of specific, yet transient protein-protein interactions. In biological systems, the detoxification of sulfite is catalyzed by the sulfite-oxidizing enzymes (SOEs), which interact with an electron acceptor for catalytic turnover. Here, we report the structural and functional analyses of the SOE S...

Journal: :Microbiology 2006
Mark Miller-Williams Peter C Loewen Ivan J Oresnik

The determinants necessary for adaptation to high NaCl concentrations and competition for nodule occupancy in Sinorhizobium meliloti were investigated genetically. Mutations in fabG as well as smc02909 (transmembrane transglycosylase), trigger factor (tig) and smc00717 (probably ftsE) gave rise to strains that were unable to tolerate high salt and were uncompetitive for nodule occupancy relativ...

2016
Mingmei Lu Zhefei Li Jianqiang Liang Yibing Wei Christopher Rensing Gehong Wei

The Sinorhizobium meliloti (S. meliloti) strain CCNWSX0020 displayed tolerance to high levels exposures of multiple metals and growth promotion of legume plants grown in metal-contaminated soil. However, the mechanism of metal-resistant strain remains unknown. We used five P1B-ATPases deletions by designating as ∆copA1b, ∆fixI1, ∆copA3, ∆zntA and ∆nia, respectively to investigate the role of P1...

Journal: :Glycobiology 2006
L A Sharypova G Chataigné N Fraysse A Becker V Poinsot

K polysaccharides (KPSs) of Sinorhizobium meliloti strains are strain-specific surface polysaccharides analogous to the group II K antigens of Escherichia coli. The K(R)5 antigen of strain AK631 is a highly polymerized disaccharide of pseudaminic and glucuronic acids. During invasion of host plants, this K antigen is able to replace the structurally different exopolysaccharide succinoglycan (EP...

Journal: :Journal of bacteriology 1999
P Aneja T C Charles

We have cloned and sequenced the 3-hydroxybutyrate dehydrogenase-encoding gene (bdhA) from Rhizobium (Sinorhizobium) meliloti. The gene has an open reading frame of 777 bp that encodes a polypeptide of 258 amino acid residues (molecular weight 27,177, pI 6.07). The R. meliloti Bdh protein exhibits features common to members of the short-chain alcohol dehydrogenase superfamily. bdhA is the first...

بشارتی, حسین, فضائلی, عاطفه,

This greenhouse experiment was carried out to evaluate the effects of salinity and bacterial inoculation on some growth indices and total protein content of alfalfa (Medicago sativa) using a factorial completely randomized design with three replications. The effect of three salinity levels (0, 6 and 12 dS/m) induced by a mixture of NaCl, CaCl2 and MgCl2 salts on growth indices and protein conte...

Journal: :Microbiology 2006
Shawn R MacLellan Allyson M MacLean Turlough M Finan

The ability to recognize and predict non-sigma54 promoters in the alphaproteobacteria is not well developed. In this study, 25 experimentally verified Sinorhizobium meliloti promoter sequences were compiled and used to predict the location of other related promoters in the S. meliloti genome. Fourteen candidate predictions were targeted for verification and of these at least 12 proved to be gen...

Journal: :Journal of bacteriology 2000
M J Soto J I Jiménez-Zurdo P van Dillewijn N Toro

Proline dehydrogenase (PutA) is a bifunctional enzyme that catalyzes the oxidation of proline to glutamate. In Sinorhizobium meliloti, as in other microorganisms, the putA gene is transcriptionally activated in response to proline. In Rhodobacter capsulatus, Agrobacterium, and most probably in Bradyrhizobium, this activation is dependent on an Lrp-like protein encoded by the putR gene, located ...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1998
G M York G C Walker

The Rhizobium meliloti ExoK and ExsH glycanases have been proposed to contribute to production of low molecular weight (LMW) succinoglycan by depolymerizing high molecular weight succinoglycan chains in R. meliloti cultures. We expressed and purified ExoK and ExsH and determined that neither enzyme can extensively cleave succinoglycan prepared from R. meliloti cultures, although neutral/heat tr...

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