Seasonal regulation of a 24-kDa protein from red-osier dogwood (Cornus sericea) xylem.
Previously, we showed that an apparent cell wall-plasma membrane interaction in xylem ray parenchyma differed between cold acclimated and non-acclimated red-osier dogwood (Cornus sericea L.) (Ristic and Ashworth 1994). For the present study, a calcium chloride extraction method was used to identify cell-wall-associated xylem proteins that accumulated during periods of cold acclimation. A 24-kDa protein represented the predominant protein in both total protein and CaCl2 extracts during cold acclimation of field-grown plants. Two-dimensional gel electrophoresis separated the 24-kDa protein into four basic isoforms. The most abundant and basic isoform had a high glycine content. In-gel digestion of this basic 24-kDa isoform generated three partial peptide fragments, of which one exhibited homology to the dehydrin protein family. An anti-dehydrin polyclonal antibody cross-reacted with the 24-kDa protein, providing further evidence that this protein is related to dehydrins. The 24-kDa protein began to accumulate in late August, reached a maximum in midwinter, declined during the spring months and was absent in early summer.
Sarnighausen
Eric
E
Department of Horticulture and Landscape Architecture, Purdue University, West Lafayette, IN 47907-1165, USA.
Karlson
Dale
D
Ashworth
Edward
E
D000064:Acclimatization / Q000502:physiology; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002122:Calcium Chloride; D003080:Cold Temperature; D029768:Cornus / Q000235:genetics / Q000502:physiology*; D004591:Electrophoresis, Polyacrylamide Gel; D015151:Immunoblotting; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D012621:Seasons; D014197:Trees / Q000235:genetics / Q000502:physiology*
D000596:Amino Acids; D010940:Plant Proteins; D002122:Calcium Chloride