title: Rice peptide deformylase PDF1B is crucial for development of chloroplasts.
abstract: Because protein synthesis begins with N-formylmethionine in plant endosymbiotic organelles, removal of the formyl group by peptide deformylase (PDF) is essential to allowing the excision of the first methionine. Rice contains three copies (OsPDF1A, OsPDF1B and OsPDF1B2) of the PDF genes. Unlike OsPDF1A and OsPDF1B, OsPDF1B2 is apparently non-functional, with several deleterious substitutions and deletions. OsPDF1A is more strongly expressed in the roots, while OsPDF1B is expressed at higher levels in mature leaves. Transient expression of PDF-green fluorescent protein (GFP) fusion proteins in the protoplasts demonstrates that, unlike OsPDF1A, OsPDF1B is localized in both the chloroplasts and the mitochondria. We used T-DNA insertional alleles to elucidate functional roles associated with OsPDF1B. Homozygous plants of pdf1b/pdf1b exhibited the phenotypes of chlorina and growth retardation. Histochemical analysis showed that the length of their mesophyll cells was increased 4- to 5-fold, resulting in a reduction in the total number of cells. Transmission electron microscopy analyses revealed that chloroplasts were severely damaged and mitochondria appeared to be mildly altered in the pdf1b mutants. Expression of genes encoded in the chloroplasts and mitochondria was altered in the mutants. Based on these results, we conclude that OsPDF1B is essential for the development of chloroplast and perhaps mitochondria.
authors: National Research Laboratory of Plant Functional Genomics, Division of Molecular and Life Sciences, Pohang University of Science and Technology (POSTECH), Pohang 790-784, Republic of Korea.
authors: Sunok
authors: S
authors: Moon
authors: Carmela
authors: C
authors: Giglione
authors: Dong-Yeon
authors: DY
authors: Lee
authors: Suyoung
authors: S
authors: An
authors: Dong-Hoon
authors: DH
authors: Jeong
authors: Thierry
authors: T
authors: Meinnel
authors: Gynheung
authors: G
authors: An
mesh_terms: D000581:Amidohydrolases / Q000235:genetics* / Q000378:metabolism; D000595:Amino Acid Sequence; D002736:Chloroplasts / Q000378:metabolism* / Q000648:ultrastructure; D017124:Conserved Sequence; D004269:DNA, Bacterial / Q000235:genetics; D018076:DNA, Complementary / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D017343:Genes, Plant; D005816:Genetic Complementation Test; D049452:Green Fluorescent Proteins / Q000235:genetics / Q000378:metabolism; D046529:Microscopy, Electron, Transmission; D008928:Mitochondria / Q000378:metabolism / Q000648:ultrastructure; D016254:Mutagenesis, Insertional; D012275:Oryza / Q000201:enzymology / Q000235:genetics* / Q000648:ultrastructure; D010641:Phenotype; D018515:Plant Leaves / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism*; D011523:Protoplasts / Q000166:cytology / Q000378:metabolism; D018749:RNA, Plant / Q000235:genetics; D020133:Reverse Transcriptase Polymerase Chain Reaction; D016415:Sequence Alignment
chemical_list: D004269:DNA, Bacterial; D018076:DNA, Complementary; D010940:Plant Proteins; D018749:RNA, Plant; C036483:T-DNA; D049452:Green Fluorescent Proteins; D000581:Amidohydrolases; C084507:peptide deformylase