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@ARTICLE{Huwa:894235,
      author       = {Huwa, Nikolai and Weiergräber, Oliver H. and Kirsch,
                      Christian and Schaffrath, Ulrich and Classen, Thomas},
      title        = {{B}iochemical and {I}nitial {S}tructural {C}haracterization
                      of the {M}onocot {C}himeric {J}acalin {O}s{JAC}1},
      journal      = {International journal of molecular sciences},
      volume       = {22},
      number       = {11},
      issn         = {1422-0067},
      address      = {Basel},
      publisher    = {Molecular Diversity Preservation International},
      reportid     = {FZJ-2021-03115},
      pages        = {5639 -},
      year         = {2021},
      abstract     = {The monocot chimeric jacalin OsJAC1 from Oryza sativa
                      consists of a dirigent and a jacalin-related lectin domain.
                      The corresponding gene is expressed in response to different
                      abiotic and biotic stimuli. However, there is a lack of
                      knowledge about the basic function of the individual domains
                      and their contribution to the physiological role of the
                      entire protein. In this study, we have established a
                      heterologous expression in Escherichia coli with high yields
                      for the full-length protein OsJAC1 as well as its individual
                      domains. Our findings showed that the secondary structure of
                      both domains is dominated by β-strand elements. Under
                      reducing conditions, the native protein displayed clearly
                      visible transition points of thermal unfolding at 59 and 85
                      °C, which could be attributed to the lectin and the
                      dirigent domain, respectively. Our study identified a single
                      carbohydrate-binding site for each domain with different
                      specificities towards mannose and glucose (jacalin domain),
                      and galactose moieties (dirigent domain), respectively. The
                      recognition of different carbohydrates might explain the
                      ability of OsJAC1 to respond to different abiotic and biotic
                      factors. This is the first report of specific
                      carbohydrate-binding activity of a DIR domain, shedding new
                      light on its function in the context of this monocot
                      chimeric jacalin.},
      cin          = {IBI-7 / IBG-1},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-7-20200312 / I:(DE-Juel1)IBG-1-20101118},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524) / 2172 - Utilization of renewable carbon and
                      energy sources and engineering of ecosystem functions
                      (POF4-217) / DFG project 369034981 - Mechanismen der durch
                      Dirigent/Jacalin-Proteinpaare hervorgerufenen
                      Breitspektrumresistenz in Pflanzen gegen pilzliche
                      Pathogene},
      pid          = {G:(DE-HGF)POF4-5241 / G:(DE-HGF)POF4-2172 /
                      G:(GEPRIS)369034981},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {34073266},
      UT           = {WOS:000660227600001},
      doi          = {10.3390/ijms22115639},
      url          = {https://juser.fz-juelich.de/record/894235},
}