Regulation of pectin methylesterase and polygalacturonate lyase activity during differentiation of infection structures in Uromyces viciae-fabae
Article Abstract:
A study of the synthesis of polygalacturonate lyase (PL) and pectin methylesterase during infection structure differentiation by the broad bean rust fungus Uromyces viciae-fabae reveals that fungal morphogenesis is necessary for the formation of the two enzymes, while PL also requires its substrate for its activation. The secretion of these cell-wall-degrading enzymes is the highest at the time of differentiation of the haustorial mother cells and infection hyphae. Limited cell-wall degradation and infection court preparation arise from a control of the amount and timing of synthesis of the enzymes and their physico-chemical properties.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
User Contributions:
Comment about this article or add new information about this topic:
Synergism between Erwinia pectate lyase isoenzymes that depolymerize both pectate and pectin
Article Abstract:
Sequencing of genomic fragments from Erwinia bacteria showed the organization of a 7.5 kbp region that encoded pectate lyase (PL) isoenzymes and found no synergism with respect to the degradation of pectate or 31% esterified pectin upon isoenzyme addition. The degradation of 31% esterified pectin by PL isoenzyme show the unconfinement of PL to the depolymerization of pectate. PL isoenzymes extend the range of pectic substrates that Erwinia can degrade.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1995
User Contributions:
Comment about this article or add new information about this topic:
The thiJ locus and its relation to phosphorylation of hydroxymethylpyrimidine in Escherichia coli
Article Abstract:
Escherichia coli produce thiamin pyrophosphate from 2-methyl-4-amino-5-hydroxymethylpyrimidine and 4-methyl-5-(beta-hydroxyethyl)thiazole via the activation of thiamin pyrophosphate-specific genes. The reaction involves the phosphorylation of hydroxymethylpyrimidine in the presence of the enzyme catalyst such as HMP kinase. Mutation experiments reveal that the thiJ locus governs the activities of HMP kinase.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1996
User Contributions:
Comment about this article or add new information about this topic:
- Abstracts: Regulation of cellular differentiation in Caulobacter crescentus
- Abstracts: Regulation of integrin alpha5beta1 affinity during myogeneic differentiation. Expression of gap junctions in cultured rat L6 cells during myogenesis
- Abstracts: Regulation of the alginate biosynthesis gene algC in Pseudomonas aeruginosa during biofilm development in continuous culture
- Abstracts: Low genetic variation among killer whales (Orcinus orca) in the Eastern North Pacific and genetic differentiation between foraging specialists
- Abstracts: Comparison of toxin overlay and solid-phase binding assays to identify diverse CryIA(c) toxin-binding proteins in Heliothis virescens midgut