Linked Life Data

17420584

Source:http://linkedlifedata.com/resource/pubmed/id/17420584

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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2007-4-23
pubmed:abstractText
Histidine-to-Aspartate (His-Asp) phosphorelay (or two-component) systems are common signal transduction mechanisms implicated in a wide variety of cellular responses to environmental stimuli in both prokaryotes and eukaryotes. For a model filamentous fungi, Aspergillus nidulans, in this study we first compiled a complete list of His-Asp phosphorelay components, including 15 genes for His-kinase (HK), four genes for response regulator (RR), and only one for histidine-containing phosphotransfer intermediate (HPt). For these RR genes, a set of deletion mutants was constructed so as to create a null allele for each. When examined these mutant strains under various conditions stressful for hyphal growth and asexual spore development, two of them (designated DeltasskA and DeltasrrA) showed a marked phenotype of hypersensitivity to oxidative stresses (particularly, to hydrogen peroxide). In this respect, expression of the vegetative-stage specific catB catalase gene was severely impaired in both mutants. Furthermore, conidia from DeltasskA were hypersensitive not only to treatment with H(2)O(2), but also to treatment at aberrantly low (4 degrees C) and high (50 degrees C) temperatures, resulting in reduced germination efficiency. In this respect, not only the catA catalase gene specific for asexual development, but also a set of genes encoding the enzymes for synthesis of certain stress tolerant compatible solutes, such as trehalose and glycerol, were markedly downregulated in conidia from DeltasskA. These results together are indicative of the physiological importance of the His-Asp phosphorelay signaling network involving the SskA and SrrA response regulators.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0916-8451
pubmed:author
pubmed:issnType
Print
pubmed:volume
71
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1003-14
pubmed:meshHeading
pubmed-meshheading:17420584-Aspartic Acid, pubmed-meshheading:17420584-Aspergillus nidulans, pubmed-meshheading:17420584-Blotting, Southern, pubmed-meshheading:17420584-Catalase, pubmed-meshheading:17420584-Culture Media, pubmed-meshheading:17420584-DNA Primers, pubmed-meshheading:17420584-Genes, Fungal, pubmed-meshheading:17420584-Histidine, pubmed-meshheading:17420584-Hydrogen Peroxide, pubmed-meshheading:17420584-Hyphae, pubmed-meshheading:17420584-In Situ Hybridization, pubmed-meshheading:17420584-Mutation, pubmed-meshheading:17420584-Oxidants, pubmed-meshheading:17420584-Oxidative Stress, pubmed-meshheading:17420584-Plasmids, pubmed-meshheading:17420584-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:17420584-Signal Transduction, pubmed-meshheading:17420584-Spores, Fungal, pubmed-meshheading:17420584-Transformation, Genetic
pubmed:year
2007
pubmed:articleTitle
The SskA and SrrA response regulators are implicated in oxidative stress responses of hyphae and asexual spores in the phosphorelay signaling network of Aspergillus nidulans.
pubmed:affiliation
Laboratory of Molecular Microbiology, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, Japan. t2706693@mbox.nagoya-u.ac.jp
pubmed:publicationType
Journal Article