Differential expression of conserved protease genes in crucifer-attacking pathovars of Xanthomonas campestris

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Standard

Differential expression of conserved protease genes in crucifer-attacking pathovars of Xanthomonas campestris. / Dow, J. M.; Fan, M. J.; Newman, M. A.; Daniels, M. J.

In: Applied and Environmental Microbiology, Vol. 59, No. 12, 1993, p. 3996-4003.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Dow, JM, Fan, MJ, Newman, MA & Daniels, MJ 1993, 'Differential expression of conserved protease genes in crucifer-attacking pathovars of Xanthomonas campestris', Applied and Environmental Microbiology, vol. 59, no. 12, pp. 3996-4003. https://doi.org/10.1128/aem.59.12.3996-4003.1993

APA

Dow, J. M., Fan, M. J., Newman, M. A., & Daniels, M. J. (1993). Differential expression of conserved protease genes in crucifer-attacking pathovars of Xanthomonas campestris. Applied and Environmental Microbiology, 59(12), 3996-4003. https://doi.org/10.1128/aem.59.12.3996-4003.1993

Vancouver

Dow JM, Fan MJ, Newman MA, Daniels MJ. Differential expression of conserved protease genes in crucifer-attacking pathovars of Xanthomonas campestris. Applied and Environmental Microbiology. 1993;59(12):3996-4003. https://doi.org/10.1128/aem.59.12.3996-4003.1993

Author

Dow, J. M. ; Fan, M. J. ; Newman, M. A. ; Daniels, M. J. / Differential expression of conserved protease genes in crucifer-attacking pathovars of Xanthomonas campestris. In: Applied and Environmental Microbiology. 1993 ; Vol. 59, No. 12. pp. 3996-4003.

Bibtex

@article{18ce5ce196ec427a890265d931f03efa,
title = "Differential expression of conserved protease genes in crucifer-attacking pathovars of Xanthomonas campestris",
abstract = "Strains of Xanthomonas campestris pathovars armoraciae and raphani, which cause leaf spotting diseases in brassicas, produce a major extracellular protease in liquid culture which was partially purified. The protease (PRT 3) was a zinc-requiring metalloenzyme and was readily distinguishable from the two previously characterized proteases (PRT 1 and PRT 2) of X. campestris pv. campestris by the pattern of degradation of β-casein and sensitivity to inhibitors. PRT 3 was produced at a low level in the vascular brassica pathogen X. campestris pv. campestris (five strains tested), in which PRT 1 and PRT 2 predominate. In contrast, expression of PRT 1, a serine protease, could not be detected in the six tested strains of the leaf spotting mesophyll pathogens. However, all these strains had DNA fragments which hybridized to a prtA probe and which probably carry a functional prtA (the structural gene for PRT 1). The structural gene for PRT 3 (prtC) was cloned by screening a genomic library of X. campestris pv. raphani in a protease- deficient X. campestris pv. campestris strain. Subcloning and Tn5 mutagenesis located the structural gene to 1.2 kb of DNA. DNA fragments which hybridized to the structural gene were found in all strains of the crucifer-attacking X. campestris pathovars tested as well as in a number of other pathovars. Experiments in which the pattern of protease production of the pathovars was manipulated by introduction of cloned genes into heterologous pathovars suggested that no determinative relationship exists between the pattern of protease gene expression and the (vascular or mesophyllic) mode of pathogenesis.",
author = "Dow, {J. M.} and Fan, {M. J.} and Newman, {M. A.} and Daniels, {M. J.}",
year = "1993",
doi = "10.1128/aem.59.12.3996-4003.1993",
language = "English",
volume = "59",
pages = "3996--4003",
journal = "Applied and Environmental Microbiology",
issn = "0099-2240",
publisher = "American Society for Microbiology",
number = "12",

}

RIS

TY - JOUR

T1 - Differential expression of conserved protease genes in crucifer-attacking pathovars of Xanthomonas campestris

AU - Dow, J. M.

AU - Fan, M. J.

AU - Newman, M. A.

AU - Daniels, M. J.

PY - 1993

Y1 - 1993

N2 - Strains of Xanthomonas campestris pathovars armoraciae and raphani, which cause leaf spotting diseases in brassicas, produce a major extracellular protease in liquid culture which was partially purified. The protease (PRT 3) was a zinc-requiring metalloenzyme and was readily distinguishable from the two previously characterized proteases (PRT 1 and PRT 2) of X. campestris pv. campestris by the pattern of degradation of β-casein and sensitivity to inhibitors. PRT 3 was produced at a low level in the vascular brassica pathogen X. campestris pv. campestris (five strains tested), in which PRT 1 and PRT 2 predominate. In contrast, expression of PRT 1, a serine protease, could not be detected in the six tested strains of the leaf spotting mesophyll pathogens. However, all these strains had DNA fragments which hybridized to a prtA probe and which probably carry a functional prtA (the structural gene for PRT 1). The structural gene for PRT 3 (prtC) was cloned by screening a genomic library of X. campestris pv. raphani in a protease- deficient X. campestris pv. campestris strain. Subcloning and Tn5 mutagenesis located the structural gene to 1.2 kb of DNA. DNA fragments which hybridized to the structural gene were found in all strains of the crucifer-attacking X. campestris pathovars tested as well as in a number of other pathovars. Experiments in which the pattern of protease production of the pathovars was manipulated by introduction of cloned genes into heterologous pathovars suggested that no determinative relationship exists between the pattern of protease gene expression and the (vascular or mesophyllic) mode of pathogenesis.

AB - Strains of Xanthomonas campestris pathovars armoraciae and raphani, which cause leaf spotting diseases in brassicas, produce a major extracellular protease in liquid culture which was partially purified. The protease (PRT 3) was a zinc-requiring metalloenzyme and was readily distinguishable from the two previously characterized proteases (PRT 1 and PRT 2) of X. campestris pv. campestris by the pattern of degradation of β-casein and sensitivity to inhibitors. PRT 3 was produced at a low level in the vascular brassica pathogen X. campestris pv. campestris (five strains tested), in which PRT 1 and PRT 2 predominate. In contrast, expression of PRT 1, a serine protease, could not be detected in the six tested strains of the leaf spotting mesophyll pathogens. However, all these strains had DNA fragments which hybridized to a prtA probe and which probably carry a functional prtA (the structural gene for PRT 1). The structural gene for PRT 3 (prtC) was cloned by screening a genomic library of X. campestris pv. raphani in a protease- deficient X. campestris pv. campestris strain. Subcloning and Tn5 mutagenesis located the structural gene to 1.2 kb of DNA. DNA fragments which hybridized to the structural gene were found in all strains of the crucifer-attacking X. campestris pathovars tested as well as in a number of other pathovars. Experiments in which the pattern of protease production of the pathovars was manipulated by introduction of cloned genes into heterologous pathovars suggested that no determinative relationship exists between the pattern of protease gene expression and the (vascular or mesophyllic) mode of pathogenesis.

UR - http://www.scopus.com/inward/record.url?scp=0027494553&partnerID=8YFLogxK

U2 - 10.1128/aem.59.12.3996-4003.1993

DO - 10.1128/aem.59.12.3996-4003.1993

M3 - Journal article

C2 - 8285704

AN - SCOPUS:0027494553

VL - 59

SP - 3996

EP - 4003

JO - Applied and Environmental Microbiology

JF - Applied and Environmental Microbiology

SN - 0099-2240

IS - 12

ER -

ID: 380059849