دورية أكاديمية
Novel glyoxysomal protein kinase, GPK1, identified by proteomic analysis of glyoxysomes in etiolated cotyledons of Arabidopsis thaliana.
| العنوان: | Novel glyoxysomal protein kinase, GPK1, identified by proteomic analysis of glyoxysomes in etiolated cotyledons of Arabidopsis thaliana. |
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| المؤلفون: | Fukao Y; Department of Cell Biology, National Institute for Basic Biology, Okazaki, 444-8585 Japan., Hayashi M, Hara-Nishimura I, Nishimura M |
| المصدر: | Plant & cell physiology [Plant Cell Physiol] 2003 Oct; Vol. 44 (10), pp. 1002-12. |
| نوع المنشور: | Comparative Study; Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Oxford University Press Country of Publication: Japan NLM ID: 9430925 Publication Model: Print Cited Medium: Print ISSN: 0032-0781 (Print) Linking ISSN: 00320781 NLM ISO Abbreviation: Plant Cell Physiol Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Tokyo : Oxford University Press Original Publication: Kyoto, Japan : Japanese Society of Plant Physiologists, |
| مواضيع طبية MeSH: | Proteome*, Arabidopsis/*enzymology , Arabidopsis/*genetics , Arabidopsis Proteins/*genetics , Glyoxysomes/*enzymology , Protein Kinases/*genetics, Amino Acid Sequence ; Arabidopsis Proteins/chemistry ; Cotyledon/enzymology ; Cotyledon/genetics ; Darkness ; Free Radical Scavengers/metabolism ; Glyoxysomes/genetics ; Hydrogen Peroxide/metabolism ; Molecular Sequence Data ; Plant Leaves/enzymology ; Plant Leaves/genetics ; Protein Kinases/chemistry ; Protein Serine-Threonine Kinases |
| مستخلص: | Glyoxysomes are present in etiolated cotyledons and contain enzymes for gluconeogenesis, which constitutes the major function of glyoxysomes. However, 281 genes seemingly related to peroxisomal functions occur in the Arabidopsis genome, implying that many unidentified proteins are present in glyoxysomes. To better understand the functions of glyoxysomes, we performed glyoxysomal proteomic analysis of etiolated Arabidopsis cotyledons. Nineteen proteins were identified as glyoxysomal proteins, including 13 novel proteins, one of which is glyoxysomal protein kinase 1 (GPK1). We cloned GPK1 cDNA by RT-PCR and characterized GPK1. The amino acid sequence deduced from GPK1 cDNA has a hydrophobic region, a putative protein kinase domain, and a possible PTS1 motif. Immunoblot analysis using fractions collected on a Percoll density gradient confirmed that GPK1 is localized in glyoxysomes. Analysis of suborganellar localization and protease sensitivity showed that GPK1 is localized on glyoxysomal membranes as a peripheral membrane protein and that the putative kinase domain is located inside the glyoxysomes. Glyoxysomal proteins are phosphorylated well in the presence of various metal ions and [g-32P]ATP, and one of them is identified as thiolase by immunoprecipitation. Immuno-inhibition of phosphorylation in glyoxysomes suggested that GPK1 phosphorylates a 40-kDa protein. These results show that protein phosphorylation systems are operating in glyoxysomes. |
| المشرفين على المادة: | 0 (Arabidopsis Proteins) 0 (Free Radical Scavengers) 0 (Proteome) BBX060AN9V (Hydrogen Peroxide) EC 2.7.- (Protein Kinases) EC 2.7.11.1 (GPK1 protein, Arabidopsis) EC 2.7.11.1 (Protein Serine-Threonine Kinases) |
| تواريخ الأحداث: | Date Created: 20031029 Date Completed: 20040212 Latest Revision: 20211203 |
| رمز التحديث: | 20221213 |
| DOI: | 10.1093/pcp/pcg145 |
| PMID: | 14581625 |
| قاعدة البيانات: | MEDLINE |
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