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1 A. vinelandii also encodes a protein designated NfuA, wh
2 A. vinelandii dsbA mutant strains were impossible to cha
4 Here, we report a systematic analysis of an A. vinelandii UW97 mutant and show that, unlike A. vinel
9 olic regulon, was replaced by the contiguous A. vinelandii iscS, iscU, iscA, hscB, hscA, fdx, and isc
12 non-polar insertion mutations within either A. vinelandii iscS or hscA revealed that such mutations
14 tudy of siderophore production in N2 -fixing A. vinelandii under a variety of trace metal conditions.
15 e its electron-flux inhibition with all four A. vinelandii nitrogenases, supporting the suggestion th
19 cy results from reduction of Fe protein from A. vinelandii (Av2) to the all-ferrous oxidation state (
21 on of His-tagged MoFe proteins purified from A. vinelandii nifZ and nifZ/nifB deletion strains DJ1182
22 mutant forms of dinitrogenase reductase from A. vinelandii that are affected in various protein activ
23 ature of the iscSUA gene cluster region from A. vinelandii is that E. coli genes previously designate
25 IscS, IscU, HscBA, and Fdx are essential in A. vinelandii and that their depletion results in a defi
27 sulfur for iron-sulfur cluster formation in A. vinelandii is supported by the presence of a cysE-lik
28 in encoded by nifD-K translational fusion in A. vinelandii is a large protein (as determined by Weste
30 a general purpose monothiol glutaredoxin in A. vinelandii, was monitored by circular dichroism spect
31 pparent co-expression of iscSUA and hscBA in A. vinelandii indicate that the proposed chaperone funct
32 existence of a redox regulatory mechanism in A. vinelandii that controls the rate of expression and m
34 ployed to confirm that the Nif- phenotype in A. vinelandii UW97 is exclusively due to the substitutio
35 at there is a putative regulatory protein in A. vinelandii that binds specifically upstream of the -3
37 -dependent regulation and gene redundancy in A. vinelandii, it has been difficult to determine the pr
39 of nitrogenase genes (nif, anf, and vnf) in A. vinelandii, and one ammonia monooxygenase gene (amoA)
40 r new prospects for the wider application of A. vinelandii as a host for the production and character
43 These results might suggest that extracts of A. vinelandii contain a physiological source of reductan
44 lementation of these assays with extracts of A. vinelandii DJ42.48 (DeltanifENX DeltavnfE) results in
45 species of VNFG are observed in extracts of A. vinelandii strains that accumulate dinitrogenase 2, w
46 or intact cluster transfer to an apo form of A. vinelandii aconitase A, a member of the monomeric deh
47 own that the [4Fe-4S] cluster-loaded form of A. vinelandii IscU, but not the [2Fe-2S] cluster-loaded
48 The redox and nitrogen-sensing functions of A. vinelandii NIFL are therefore separable and are discr
49 unlike A. vinelandii DJ54, the nifH gene of A. vinelandii UW97 has no deletion in either coding sequ
51 ave no effects on the diazotrophic growth of A. vinelandii while WO(3) NPs are highly detrimental to
52 L clusters to the biosynthetic machinery of A. vinelandii for further maturation into the M clusters
53 elective pressure against the maintenance of A. vinelandii iscS or hscA knock-out mutations and sugge
54 erefore, it seems that the Nif- phenotype of A. vinelandii UW97 is caused by a general structural dis
55 tation responsible for the Nif- phenotype of A. vinelandii UW97 is the substitution of a non-conserve
59 re we report the complete genome sequence of A. vinelandii DJ, which has a single circular genome of
60 aining extracts from a DeltanifHDK strain of A. vinelandii CA12 along with FeMoco, Fe protein, and Mg
63 d DNA sequence analysis of a 7,886-base pair A. vinelandii genomic segment that includes the iscS gen
64 with exquisitely oxygen-sensitive processes, A. vinelandii is specialized in terms of its complement
69 eam of Escherichia coli fpr, suggesting that A. vinelandii may have a SoxS-like regulatory system and
73 on of reductant is required, however, if the A. vinelandii cell-free extract is chemically oxidized p
74 gene, herein designated fdxD, that is in the A. vinelandii iscSUA operon that encodes proteins involv
75 rrangement observed in the structures of the A. vinelandii and C. pasteurianum Fe-proteins indicate t
76 eporter gene was placed under control of the A. vinelandii fpr promoter and introduced into wild type
78 was used for the functional analysis of the A. vinelandii isc genes, whose products are involved in
79 Here, we report the identification of the A. vinelandii protein that binds specifically to the par
80 dients during turnover demonstrates that the A. vinelandii cytochrome bd oxidase is coupled to energy
82 sults show that the toxicity of WO(3) NPs to A. vinelandii is due to an interference with the catecho
83 350 times tighter than that of the wild-type A. vinelandii nitrogenase complex and at least 20 times
84 ructure of the complex between the wild-type A. vinelandii nitrogenase proteins stabilized with ADP.A
85 vinelandii UW97 mutant and show that, unlike A. vinelandii DJ54, the nifH gene of A. vinelandii UW97
86 e relative levels of FdIV and FdI in various A. vinelandii strains leading to the conclusion that FdI
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