Comparative Proteomics Study on Anther Mitochondria between Cytoplasmic Male Sterility Line and its Maintainer in Kenaf ( L.)

摘要

Cytoplasmic male sterility (CMS) is a maternally inherited trait that causes the inability to produce functional pollen during anther development. Cytoplasmic male sterility is considered to be caused by mitochondrial mutation and regarded as a perfect model system for the investigation of nucleus-cytoplasmic interaction. Kenaf CMS was first found by our group, but little has been known about the molecular mechanism. To reveal the possible mechanism, a comparative proteomic analysis of kenaf anther mitochondria from a CMS line and its maintainer was conducted. Changes in the abundance of proteins were examined using two-dimensional (2-D) electrophoresis. Among the 1000 protein spots reproducibly detected on each gel, 50 proteins were found differentially regulated (p 0.05, change fold 1.5). Identified by matrix-assisted-laser-desorption-time-of-flight mass spectrometry MALDI-TOF/TOF-MS technology, 22 proteins were characterized. These proteins were involved in adenosine triphosphate (ATP) synthesis and energy metabolism, cytoskeleton, chaperones and protein processing, transmembrane transport, transcription, and other functions. The quantitative real time polymerase chain reaction (PCR) results of some differential proteins showed consistency between transcripts and proteins. Confined mostly to downregulated proteins in the respiratory chain, the anther respiratory rate investigation showed it was extremely decreased in the CMS line.