Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Brenda K. Scholz-Schroeder"'
Publikováno v:
Molecular Plant-Microbe Interactions, Vol 16, Iss 4, Pp 271-280 (2003)
Syringopeptin is a necrosis-inducing phytotoxin, composed of 22 amino acids attached to a 3-hydroxy fatty acid tail. Syringopeptin, produced by Pseudomonas syringae pv. syringae, functions as a virulence determinant in the plant-pathogen interaction.
Externí odkaz:
https://doaj.org/article/3e4f2f8778a449469fb5b41b6cb3afbd
Publikováno v:
Molecular Plant-Microbe Interactions, Vol 15, Iss 1, Pp 43-53 (2002)
Sequence analysis of the right border of the syr gene cluster of Pseudomonas syringae pv. syringae strain B301D revealed the presence of the salA gene 8,113 bp downstream of syrE. The predicted SalA protein of strain B301D differs by one amino acid f
Externí odkaz:
https://doaj.org/article/4f6cdb604637458b97fda3726b284a7e
Publikováno v:
Molecular Plant-Microbe Interactions, Vol 14, Iss 12, Pp 1426-1435 (2001)
Genetic and phenotypic mapping of an approximately 145-kb DraI fragment of Pseudomonas syringae pv. syringae strain B301D determined that the syringomycin (syr) and syringopeptin (syp) gene clusters are localized to this fragment. The syr and syp gen
Externí odkaz:
https://doaj.org/article/1d4909a1f74c4bb494947b868a45be64
Publikováno v:
Molecular Plant-Microbe Interactions, Vol 14, Iss 3, Pp 336-348 (2001)
Sequencing of an approximately 3.9-kb fragment downstream of the syrD gene of Pseudomonas syringae pv. syringae strain B301D revealed that this region, designated sypA, codes for a peptide synthetase, a multifunctional enzyme involved in the thiotemp
Externí odkaz:
https://doaj.org/article/a0d7f672fd724d779afc56d6a2f7757c
Publikováno v:
Pseudomonas ISBN: 9780306483769
Pseudomonas syringae elicits a variety of symptoms on plants, including cankers, leaf spots, and galls, and is divided into pathogenic variants (pathovars; pv.) that vary in host range. The infection of host plants by P syringae is a multi-step proce
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::96783603ae2428d555f3805c86b84541
https://doi.org/10.1007/978-1-4419-9084-6_4
https://doi.org/10.1007/978-1-4419-9084-6_4
Publikováno v:
Molecular plant-microbe interactions : MPMI. 16(4)
Syringopeptin is a necrosis-inducing phytotoxin, composed of 22 amino acids attached to a 3-hydroxy fatty acid tail. Syringopeptin, produced by Pseudomonas syringae pv. syringae, functions as a virulence determinant in the plant-pathogen interaction.
Publikováno v:
Pseudomonas syringae and related pathogens ISBN: 9789048162673
Pseudomonas syringae pv. syringae produces two classes of pore-forming lipodepsipeptide phytotoxins that target host plasma membranes. Both syringomycin and syringopeptin are synthesised by modular nonribosomal peptide synthetases. The syringomycin (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f2eb86816cd891747f69abecbe9f1c13
https://doi.org/10.1007/978-94-017-0133-4_15
https://doi.org/10.1007/978-94-017-0133-4_15
Publikováno v:
FEMS microbiology letters. 210(1)
Characterization of the biological roles of proteins is essential for functional genomics of pseudomonads. Heterologous proteins overproduced in Escherichia coli frequently fail to exhibit biological function. To circumvent this problem, vector pMEKm
Publikováno v:
Molecular plant-microbe interactions : MPMI. 15(1)
Sequence analysis of the right border of the syr gene cluster of Pseudomonas syringae pv. syringae strain B301D revealed the presence of the salA gene 8,113 bp downstream of syrE. The predicted SalA protein of strain B301D differs by one amino acid f
Genetic and phenotypic mapping of an approximately 145-kb DraI fragment of Pseudomonas syringae pv. syringae strain B301D determined that the syringomycin (syr) and syringopeptin (syp) gene clusters are localized to this fragment. The syr and syp gen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4f88e148d5edab36830297efe4bd674d
http://hdl.handle.net/11573/94379
http://hdl.handle.net/11573/94379