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Analysis of AtHIRD11 Intrinsic Disorder and Binding Towards Metal Ions by Capillary Gel Electrophoresis and Affinity Capillary Electrophoresis
Published on: August 22, 2018
Quantitative analysis of auxin-regulated proteins from basal part of leaf sheaths in rice by two-dimensional
Fang Shi1, Hironori Takasaki, Setsuko Komatsu
1National Institute of Crop Science, 2-1-18 Kannondai, Tsukuba 305-8518, Japan.
Abstract:
To identify the effects of auxin on rice root formation, proteins induced by exogenous addition of auxin to rice seedlings were analyzed by a proteomic approach. Root formation by rice seedlings was promoted by 0.45microM 2,4-dichlorophenoxyacetic acid (2,4-D) and repressed by 60microM p-chlorophenoxyisobutyric acid (PCIB). Proteins extracted from the basal part of leaf sheaths of rice seedlings treated with 2,4-D or PCIB for 48h were labeled with Cy3 and Cy5, and separated by two-dimensional polyacrylamide gel electrophoresis. Out of nine proteins up-regulated by 2,4-D and down-regulated by PCIB, five proteins showing significant difference in abundance were used for expression analysis at the transcript abundance level. Transcript abundance of the mitochondrial complex I subunit slightly increased with 2,4-D treatment and were repressed by PCIB. The transcript abundance of EF-1beta', myosin heavy chain and mitochondrial [Mn]SOD increased with 2,4-D treatment but did not decrease with PCIB. The transcript abundance of aldehyde dehydrogenase was not effected by 2,4-D or PCIB. These results indicate that mitochondrial complex I subunit is part of the downstream signal cascade of PCIB, whereas myosin heavy chain, mitochondrial [Mn]SOD and EF-1beta' are involved in the 2,4-D signal cascade but are probably upstream of PCIB.

