LEA proteins and the evolution of the WHy domain

dc.contributor.authorMertens, Jasmin
dc.contributor.authorAliyu, Habibu
dc.contributor.authorCowan, Don A.
dc.contributor.emaildon.cowan@up.ac.zaen_ZA
dc.date.accessioned2018-08-21T11:58:04Z
dc.date.issued2018-05
dc.description.abstractThe LEA family is composed of a diverse collection of multi-domain and multi-functional proteins, found in all three Domains of the Tree of Life, but particularly common in plants. Most members of the family are known to play an important role in abiotic stress response and stress tolerance in plants, but are also part of the plant hypersensitive response to pathogen infection. The mechanistic basis for LEA protein functionality is still poorly understood. The group of LEA 2 proteins harbour one or more copies of a unique domain, the [underln]W[/underln]ater stress and [underln]Hy[/underln]persensitive response (WHy) domain. This domain sequence has recently been identified as a unique ORF in some bacterial genomes (mostly in the phylum Firmicutes), and the recombinant bacterial WHy protein has been shown to exhibit a stress tolerance phenotype in E. coli and an in vitro protein denaturation protective function. Multi-domain phylogenetic analyses suggest that the WHy protein gene sequence may have ancestral origins in the Domain Archaea, with subsequent acquisition in Bacteria and Eukaryotes via endosymbiont or Horizontal Gene Transfer mechanisms.en_ZA
dc.description.departmentBiochemistryen_ZA
dc.description.departmentGeneticsen_ZA
dc.description.departmentMicrobiology and Plant Pathologyen_ZA
dc.description.embargo2018-11-01
dc.description.librarianhj2018en_ZA
dc.description.sponsorshipThe University of Pretoria, the South African Technology Innovation Agency, and the National Research Foundation.en_ZA
dc.description.urihttp://aem.asm.orgen_ZA
dc.identifier.citationMertens, J., Aliyu, H. & Cowan, D.A. 2018, 'LEA proteins and the evolution of the WHy domainLEA proteins and the evolution of the WHy domain', Applied and Environmental Microbiology, vol. 84, no. 15, AEM.00539-18.en_ZA
dc.identifier.issn0099-2240 (print)
dc.identifier.issn1098-5336 (online)
dc.identifier.other10.1128/AEM.00539-18
dc.identifier.urihttp://hdl.handle.net/2263/66302
dc.language.isoenen_ZA
dc.publisherAmerican Society for Microbiologyen_ZA
dc.rights© 2018, American Society for Microbiology. All Rights Reserved.en_ZA
dc.subjectWHy proteinen_ZA
dc.subjectWater hypersensitive domainen_ZA
dc.subjectPlantsen_ZA
dc.subjectBacteriaen_ZA
dc.subjectFrosten_ZA
dc.subjectCold-/freeze-stressen_ZA
dc.subjectDroughten_ZA
dc.subjectDehydrinsen_ZA
dc.subjectAbiotic stressen_ZA
dc.subjectLate abundant embryogenesis proteinen_ZA
dc.subjectIdentificationen_ZA
dc.subjectDrought stressen_ZA
dc.subjectDehydrinen_ZA
dc.subjectIn vitroen_ZA
dc.subjectHigher plantsen_ZA
dc.subjectCryoprotective activityen_ZA
dc.subjectPhylogenetic analysisen_ZA
dc.subjectMessenger ribonucleic aciden_ZA
dc.subjectArabidopsis thalianaen_ZA
dc.titleLEA proteins and the evolution of the WHy domainen_ZA
dc.typePostprint Articleen_ZA

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