Results 111 to 120 of about 1,472 (156)

Dynamic Executors of Bacterial Signals: Functional Versatility and Regulatory Networks of c-di-GMP Effectors. [PDF]

open access: yesBiomolecules
Jia J   +11 more
europepmc   +1 more source

Proline iminopeptidase gene from Xanthomonas campestris pv. citri [PDF]

open access: yesMicrobiology (United Kingdom), 1996
The pip gene coding for the proline iminopeptidase (Pip) of Xanthomonas campestris pv. citri was cloned in an Escherichia coli leuB strain using a selective medium containing the dipeptide D-Ala-L-Leu as the sole source of L-leucine. Nucleotide sequencing of this gene revealed a 939 bp open reading frame encoding a 312 amino acid protein (35 126 Da ...
Jana Alonso, JOSÉ L Garcia
exaly   +3 more sources

Detection of Xanthomonas campestris pv. citri by the polymerase chain reaction method [PDF]

open access: yesApplied and Environmental Microbiology, 1993
pFL1 is a pUC9 derivative that contains a 572-bp EcoRI insert cloned from plasmid DNA of Xanthomonas campestris pv. citri XC62. The nucleotide sequence of pFL1 was determined, and the sequence information was used to design primers for application of the polymerase chain reaction (PCR) to the detection of X. campestris pv.
John S Hartung
exaly   +5 more sources
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Structural and functional characterization of the lexA gene of Xanthomonas campestris pathovar citri

Molecular Genetics and Genomics, 2001
The role of the LexA protein and, specifically, its effect on recA expression were analyzed in Xanthomonas campestris pathovar citri (X.c. pv. citri). Overexpression of LexA from X.c. pv. citri, in the plant pathogen, as well as in Escherichia coli, results in increased sensitivity to the DNA-damaging agents mitomycin C and ultraviolet radiation ...
Tsong-Teh Kuo
exaly   +3 more sources

Structure of proline iminopeptidase from Xanthomonas campestris pv. citri: a prototype for the prolyl oligopeptidase family [PDF]

open access: yesEMBO Journal, 1998
The proline iminopeptidase from Xanthomonas campestris pv. citri is a serine peptidase that catalyses the removal of N-terminal proline residues from peptides with high specificity. We have solved its three-dimensional structure by multiple isomorphous replacement and refined it to a crystallographic R-factor of 19.2% using X-ray data to 2.7 A ...
FRANCISCO J Medrano   +2 more
exaly   +3 more sources

Identification of a lexA Gene in, and Construction of a lexA Mutant of, Xanthomonas campestris pv. citri

Current Microbiology, 2000
The lexA gene of Xanthomonas campestris pathovar citri (X.c. pv. citri) was cloned and sequenced. The 639-bp open reading frame encodes a protein of 213 amino acids that shares substantial sequence homology with the products of previously characterized lexA genes, sharing 46% identity with the LexA protein of Escherichia coli.
Mei-Kwei Yang
exaly   +3 more sources

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