ライフサイエンスコーパス: R. meliloti

1 R. meliloti ChvI may serve as the response regulator of

2 R. meliloti derivatives carrying insertion mutations in

3 ulation with Rhizobium meliloti or by adding R. meliloti-produced nodulation (Nod) factors or the pla

4 els during all stages of symbiosis, allowing R. meliloti cells to be visualized as they grew in the r

5 Finally, the C. crescentus and R. meliloti ccrM genes are functionally interchangeable,

6 from those of other strains of R. fredii and R. meliloti, and this finding provides further evidence

7 acid changes between A. tumefaciens FtsA and R. meliloti FtsA do not prevent their direct interaction

8 atory proteins: ExoX of Rhizobium NGR234 and R. meliloti, and Psi of R. leguminosarum bv. phaseoli.

9 Furthermore, while the A. tumefaciens and R. meliloti donors produced high levels of the autoinduc

10 In at least two alpha subdivision bacteria, R. meliloti and C. crescentus, CcrM-mediated methylation

11 bacterium C. crescentus, the soil bacterium R. meliloti, and the intracellular pathogen B. abortus s

12 within plant cells in the symbiosis between R. meliloti and alfalfa.

13 n the establishment of the symbiosis between R. meliloti Rm1021 and its host plant, alfalfa.

14 Thus, in both R. meliloti and C. crescentus, CcrM methylation is an in

15 inoglycan that is being produced actively by R. meliloti, but not succinoglycan that has accumulated

16 sufficient to mediate successful invasion by R. meliloti mutants which fail to produce EPS, implying

17 or regulation of succinoglycan production by R. meliloti through the ExoS-ChvI two-component regulato

18 ion of low-molecular-weight succinoglycan by R. meliloti.

19 ected, GFP-tagged FtsZ1 and FtsA from either R. meliloti or A. tumefaciens localized to the division

20 tensively cleave succinoglycan prepared from R. meliloti cultures, although neutral/heat treatment an

21 One approach to understanding how R. meliloti alters its physiology in order to become an

22 igh molecular weight succinoglycan chains in R. meliloti cultures.

23 Production of EPS in R. meliloti is likely controlled at several levels.

24 ent depolymerization activities expressed in R. meliloti cultures.

25 Overproduction of E. coli FtsZ in R. meliloti resulted in the same branched morphology, as

26 was no counterpart FlaC protein reported in R. meliloti, but the A. tumefaciens FlaC is similar in a

27 ular weight distribution of succinoglycan in R. meliloti cultures is determined by both the levels of

28 l role in production of LMW succinoglycan in R. meliloti cultures.

29 Transfer of pIJ1848 into R. meliloti 1021 results in heterologous expression of a

30 By screening ca. 100,000 Tn5-mutagenized R. meliloti bacteria for resistance to bacteriophage phi

31 t shared the unusual C-terminal extension of R. meliloti FtsZ1 was found in A. tumefaciens.

32 Distinct from FlaA and FlaB of R. meliloti is the absence of histidine and cysteine res

33 no acid residues fewer than FlaA and FlaB of R. meliloti).

34 on of specific low molecular weight forms of R. meliloti exported and surface polysaccharides, includ

35 rate and determine the patterns of growth of R. meliloti residing inside its host plant.

36 ng transposon mutagenesis of exoK mutants of R. meliloti and screening for colonies with even more se

37 ranched morphology, as did overproduction of R. meliloti FtsZ in Agrobacterium tumefaciens.

38 When A. tumefaciens FtsA-GFP or R. meliloti FtsA-GFP was expressed in E. coli, they fail

39 ting that FtsA from either A. tumefaciens or R. meliloti can bind directly to its cognate FtsZ.

40 ed at high levels in intracellular symbiotic R. meliloti and at low levels in the free-living bacteri

41 A. thaliana reductases, the histidine-tagged R. meliloti cysH gene product appears to favor APS over

42 e demonstrated by Western blot analyses that R. meliloti expresses ExoK and ExsH, that both proteins

43 s, we have obtained evidence indicating that R. meliloti has genetically separable systems for the sy

44 The R. meliloti bacA386::Tn(pho)A mutant, as well as a newly

45 genesis of challenge phages that carried the R. meliloti nifH promoter, mutant phages that could form

46 ogens of mammals, it is not required for the R. meliloti-alfalfa symbiosis.

47 box which shows several differences from the R. meliloti nod box consensus sequence.

48 ggests that EPS plays a specific role in the R. meliloti-M. sativa symbiosis.

49 a highly conserved B. abortus homolog of the R. meliloti bacA gene, which encodes a putative cytoplas

50 ns chvI homolog located just upstream of the R. meliloti exoS gene.

51 In order to determine the specificity of the R. meliloti reductase, the R. meliloti cysH homolog was

52 n to identify genes under the control of the R. meliloti regulatory protein NodD3, SyrM, or SyrA.

53 essed in E. coli with the lacZ promoter, the R. meliloti bacA gene was found to suppress all the know

54 pecificity of the R. meliloti reductase, the R. meliloti cysH homolog was histidine tagged and purifi

55 laC is similar in amino acid sequence to the R. meliloti FlaA (59.8% identity) and FlaB (66.7% identi

56 in Escherichia coli and purified, as was the R. meliloti ChvI protein.

57 allenge phages were constructed in which the R. meliloti nifH promoter replaced the binding site for

58 whether this preference for APS is unique to R. meliloti among members of the family Rhizobiaceae or

59 Using R. meliloti cells that express green fluorescent protein

60 When R. meliloti FtsZ1-GFP or A. tumefaciens FtsZ-GFP was exp

61 ene products whose expression decreases when R. meliloti becomes an intracellular symbiont.

62 However, when R. meliloti FtsZ1 was coexpressed with them, fluorescenc

63 i cell division machinery, we tested whether R. meliloti cells could also form long filaments after c