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Differences in Freeze Tolerance of Zoysiagrasses: I. Role of Proteins

^a Dep. of Horticulture, Univ. of Arkansas, 316 Plant Sciences Bldg., Fayetteville, AR 72701
^b Dep. of Agronomy, Purdue Univ., 915 W. State St., West Lafayette, IN 47907-2054. Purdue Univ. Agriculture Experiment Station Journal no. 2006-18051

View larger version (34K): [in this window] [in a new window]   Figure 1. Buffer-soluble protein concentrations as influenced by cold acclimation and zoysiagrass cultivar. Error bars represent one standard error of the mean (n = 6). Species is indicated by (m) or (j) for Zoysia matrella or Z. japonica, respectively.

View larger version (70K): [in this window] [in a new window]   Figure 2. Sodium dodecylsulfate polyacrylamide gel electrophoresis (SDS-PAGE) profiles and immunoblots of buffer-soluble protein from zoysiagrass genotypes with different freeze tolerances. Gels show buffer-soluble protein profiles from nonacclimated (Lanes 2–14) and cold-acclimated (Lanes 15–27) zoysiagrass plants. Gels were loaded with equal amounts of buffer-soluble protein (25 µg) per lane. Gels were first stained with (A) Coomassie brilliant blue R-250 and then (B) Ag stained. Solid lines indicate predominant proteins present in nonacclimated and cold-acclimated plants and dashed lines indicated protein changes in response to cold acclimation with their predicted molecular masses (A and B, far right). (C) Immunoblots show 23- and 25-kDa dehydrin-like polypeptides probed with a 1:250 dilution of rabbit antidehydrin polyclonal primary antibody. ‘White icicle’ radish (Raphanus sativus) seed was used as a positive control with 3 µg of protein loaded in Lane 1. Solid lines indicate dehydrin-like polypeptides and their predicted molecular masses (C, far right). Molecular weight (MW) markers represent proteins sized 104, 81, 48, 36, 27, and 19 kDa (A, B, and C, far left).

View larger version (46K): [in this window] [in a new window]   Figure 3. Immunoblots of buffer-soluble protein from zoysiagrass genotypes with different freeze tolerances. Immunoblots show dehydrin-like polypeptides probed with a 1:333 dilution of antidehydrin polyclonal primary antibody for nonacclimated (NA: Lanes 3, 5, 7, and 9) and cold-acclimated (CA: Lanes 4, 6, 8, and 10) zoysiagrass plants. Equal amounts of protein (25 µg) were loaded into each lane. Radish (Raphanus sativus) seed was used as a positive control with 10 µg of protein loaded in Lane 2. Dehydrin-like polypeptides and their predicted molecular masses are indicated (far right). Molecular weight (MW) markers represent proteins sized 104, 81, 48, 36, 27, and 19 kDa (Lane 1).

View larger version (22K): [in this window] [in a new window]   Figure 4. (A) Immunoblot of a 23-kDa dehydrin-like polypeptide from zoysiagrass genotypes with different freeze tolerances, showing a 23-kDa dehydrin probed with a 1:250 dilution of antidehydrin polyclonal primary antibody for cold-acclimated plants. Equal amounts of protein (25 µg) were loaded in each lane. (B) There was a relationship (r2 = 0.41, P = 0.018) between freeze tolerance (LT50, the lethal temperature killing 50% of the plants) and optical density (O.D.) of the 23-kDa dehydrin-like polypeptide band.

View larger version (20K): [in this window] [in a new window]   Figure 5. (A) Immunoblot of a 25-kDa dehydrin-like polypeptide from zoysiagrass genotypes with different freeze tolerances, showing a 25-kDa dehydrin probed with a 1:250 dilution of antidehydrin polyclonal primary antibody for cold-acclimated plants. Equal amounts of protein (25 µg) were loaded in each lane. (B) There was no correlation (r = 0.47, P = 0.11) between freeze tolerance (LT50, the lethal temperature killing 50% of the plants) and optical density (O.D.) of the 25-kDa dehydrin band.