A single amino acid substitution beyond the C2H2-zinc finger in Ros derepresses virulence and T-DNA genes in Agrobacterium tumefaciens

Archdeacon, J

doi:10.1016/s0378-1097(00)00197-x

Cited by 3 publications

(4 citation statements)

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“…The mutation in the ros gene present in the spontaneous mutant 4011R of A. tumefaciens has been shown to be a single substitution of one of the basic residues of BR4, Arg125, with a cysteine (29). Interestingly, this mutation abolishes the protein DNA binding capability, already suggesting a possible role in DNA binding for Arg125.…”

Section: Resultsmentioning

confidence: 99%

“…Whether the other zinc coordinating residues, and especially both the second and the third histidine residues, were important for DNA binding activity remained to be determined. More recently, an amino acid substitution close to the carboxy terminus of Ros which causes loss of the protein DNA binding activity has been identified, suggesting that residues outside of the zinc finger also interact with DNA or are important in maintaining the conformational integrity of the Ros DNA binding domain (29).…”

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A Novel Type of Zinc Finger DNA Binding Domain in the Agrobacterium tumefaciens Transcriptional Regulator Ros

et al. 2006

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Transcriptional factors bearing a Cys(2)His(2) zinc finger were thought to be confined to eukaryotes, but recent studies have suggested their presence also in prokaryotes. In this paper, we report the first complete functional characterization of the DNA binding domain present in the putative Cys(2)His(2) zinc finger-containing prokaryotic transcriptional regulator Ros from Agrobacterium tumefaciens. We demonstrate that in the single zinc binding motif present in the Ros protein the metal ion is coordinated by two cysteines (Cys79 and Cys82) and two histidines (His92 and His97), separated by a shorter spacer with respect to the eukaryotic classical Cys(2)His(2) domains. The Cys(2)His(2) zinc finger motif is essential for Ros DNA binding and is part of a larger DNA binding domain which includes four basic regions located on either side of the finger, one at the N-terminus and three at the C-terminus. The one described here is a novel type of DNA binding domain containing a noncanonical Cys(2)His(2) zinc finger motif which, by sequence alignment, seems to be conserved in all the bacterial putative zinc finger proteins identified so far. Interestingly, basic amino acids have been shown to be important in stabilizing the DNA binding of eukaryotic single Cys(2)His(2) zinc finger domains, confirming that the modality of DNA binding using a single zinc finger motif flanked by basic residues is widespread throughout the living kingdom from eukaryotic, both animal and plant, to prokaryotic, even if in each kingdom it presents its peculiarity.

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Section: Resultsmentioning

confidence: 99%

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A Novel Type of Zinc Finger DNA Binding Domain in the Agrobacterium tumefaciens Transcriptional Regulator Ros

et al. 2006

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“…The first identified zinc finger domain in prokaryotes is Ros from Agrobacterium tumefaciens and this 15.5 kDa protein, with a coordinating zinc ion, serves as a transcriptional regulator. Ros mutational studies proved that the zinc finger domain negatively controls virC and virD operons that regulate the oncogene-bearing region in the T-DNA of the T1 plasmid [1,14]. This signaling cascade finally suppresses ipt in the plant.…”

Section: Classical Zinc Fingers In Prokaryotesmentioning

confidence: 99%

Structural Analyses of Zinc Finger Domains for Specific Interactions with DNA

Eom¹,

Cheong²,

Lee³

2016

Journal of Microbiology and Biotechnology

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Zinc finger proteins are among the most extensively applied metalloproteins in the field of biotechnology owing to their unique structural and functional aspects as transcriptional and translational regulators. The classical zinc fingers are the largest family of zinc proteins and they provide critical roles in physiological systems from prokaryotes to eukaryotes. Two cysteine and two histidine residues (Cys₂His₂) coordinate to the zinc ion for the structural functions to generate a ββα fold, and this secondary structure supports specific interactions with their binding partners, including DNA, RNA, lipids, proteins, and small molecules. In this account, the structural similarity and differences of well-known Cys₂His₂-type zinc fingers such as zinc interaction factor 268 (ZIF268), transcription factor IIIA (TFIIIA), GAGA, and Ros will be explained. These proteins perform their specific roles in species from archaea to eukaryotes and they show significant structural similarity; however, their aligned amino acids present low sequence homology. These zinc finger proteins have different numbers of domains for their structural roles to maintain biological progress through transcriptional regulations from exogenous stresses. The superimposed structures of these finger domains provide interesting details when these fingers are applied to specific gene binding and editing. The structural information in this study will aid in the selection of unique types of zinc finger applications in vivo and in vitro approaches, because biophysical backgrounds including complex structures and binding affinities aid in the protein design area.

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“…Although the T-DNA is weakly transcribed in A. tumefaciens (Gelvin et al, 1981), the ipt gene located in the T-DNA that encodes isopentenyltransferase activity is not fully expressed in A. tumefaciens (Heinemeyer et al, 1987). It was later shown that the Ipt gene was repressed by a eukaryotic-like zinc-finger protein called Ros encoded by the chromosomal ros gene of A. tumefaciens (Chou et al, 1998) and derepressed by a single amino acid substitution of Ros (Archdeacon et al, 2006). Nuclear magnetic resonance spectroscopic studies of Ros revealed a novel DNA recognition mechanism of eukaryotic promoters (Malgieri et al, 2007).…”

Section: An Extrachromosomal Element Confers Virulence On a Tumefaciensmentioning

confidence: 99%

Historical account on gaining insights on the mechanism of crown gall tumorigenesis induced by Agrobacterium tumefaciens

Kado

2014

Front. Microbiol.

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The plant tumor disease known as crown gall was not called by that name until more recent times. Galls on plants were described by Malpighi (1679) who believed that these extraordinary growth are spontaneously produced. Agrobacterium was first isolated from tumors in 1897 by Fridiano Cavara in Napoli, Italy. After this bacterium was recognized to be the cause of crown gall disease, questions were raised on the mechanism by which it caused tumors on a variety of plants. Numerous very detailed studies led to the identification of Agrobacterium tumefaciens as the causal bacterium that cleverly transferred a genetic principle to plant host cells and integrated it into their chromosomes. Such studies have led to a variety of sophisticated mechanisms used by this organism to aid in its survival against competing microorganisms. Knowledge gained from these fundamental discoveries has opened many avenues for researchers to examine their primary organisms of study for similar mechanisms of pathogenesis in both plants and animals. These discoveries also advanced the genetic engineering of domesticated plants for improved food and fiber.

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A single amino acid substitution beyond the C2H2-zinc finger in Ros derepresses virulence and T-DNA genes in Agrobacterium tumefaciens

Cited by 3 publications

References 20 publications

A Novel Type of Zinc Finger DNA Binding Domain in the Agrobacterium tumefaciens Transcriptional Regulator Ros

A Novel Type of Zinc Finger DNA Binding Domain in the Agrobacterium tumefaciens Transcriptional Regulator Ros

Structural Analyses of Zinc Finger Domains for Specific Interactions with DNA

Historical account on gaining insights on the mechanism of crown gall tumorigenesis induced by Agrobacterium tumefaciens

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