| Abstract Detail
Growth and Vegetative Development Sunok, Moon [1], Suyoung, An [2], Lee, Dong-Yeon [2], An, Gynheung [2]. Characterization of the peptide deformylases in rice. Because protein synthesis begins with N-formyl methionine in plant endosymbiotic organelles, removal of the formyl group by peptide deformylase (PDF) is essential for maintenance of life. In rice there are three copies (OsPDF1A, OsPDF1B1 and OsPDF1B2) of the PDF genes that were expressed in all the organs examined. Whereas OsPDF1A was more strongly expressed in young seedlings, the OsPDF1B genes were expressed at higher levels in mature plants. Transient expression of PDF:green fluorescence (GFP) fusion proteins in mesophyll protoplasts showed that OsPDF1A was localized in chloroplasts while OsPDF1B1 and OsPDF1B2 were present in both chloroplasts and mitochondria. We elucidated functional roles of the OsPDF1B1 gene using two T-DNA insertional alleles. The pdfb1/pdfb1 homozygous plants exhibited the phenotypes of chlorina and growth retardation. Histochemical analysis exhibited that the length of mesophyll cells was increased about three-fold, resulting in reduction in a total number of the cells. Transmission electron microscopy analyses revealed that not only chloroplasts but also mitochondria were damaged in pdf1b1. Expression of genes that are encoded in chloroplasts and mitochondria was altered in the mutant. Based on these results, we conclude that OsPDF1B1 is essential for development of chloroplasts and mitochondria. Log in to add this item to your schedule
1 - Pohang University of Science and Technology (POSTECH), Division of Molecular and Life Sciences, Pohang, 790, Republic of Korea 2 - Pohang University of Science and Technology (POSTECH), Division of Molecular and Life Sciences
Keywords: peptide deformylase Chloroplast mitochondria chlorina growth retardation.
Presentation Type: Plant Biology Abstract Session: P Location: Exhibit Hall (Northeast, Southwest & Southeast)/Hilton Date: Sunday, July 8th, 2007 Time: 8:00 AM Number: P26017 Abstract ID:387 |