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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Barkan, A. Roy, L. M. |
| Description | Author Affiliation: Roy LM ( Institute of Molecular Biology, University of Oregon, Eugene, Oregon 97403, USA.) |
| Abstract | Results of in vitro and genetic studies have provided evidence for four pathways by which proteins are targeted to the chloroplast thylakoid membrane. Although these pathways are initially engaged by distinct substrates and involve some distinct components, an unresolved issue has been whether multiple pathways converge on a common translocation pore in the membrane. A homologue of eubacterial SecY called cpSecY is localized to the thylakoid membrane. Since SecY is a component of a protein-translocating pore in bacteria, cpSecY likely plays an analogous role. To explore the role of cpSecY, we obtained maize mutants with transposon insertions in the corresponding gene. Null cpSecY mutants exhibit a severe loss of thylakoid membrane, differing in this regard from mutants lacking cpSecA. Therefore, cpSecY function is not limited to a translocation step downstream of cpSecA. The phenotype of cpSecY mutants is also much more pleiotropic than that of double mutants in which both the cpSecA- and ΔpH-dependent thylakoid-targeting pathways are disrupted. Therefore, cpSecY function is likely to extend beyond any role it might play in these targeting pathways. CpSecY mutants also exhibit a defect in chloroplast translation, revealing a link between chloroplast membrane biogenesis and chloroplast gene expression. |
| ISSN | 00219525 |
| e-ISSN | 15408140 |
| Journal | The Journal of Cell Biology |
| Issue Number | 2 |
| Volume Number | 141 |
| Language | English |
| Publisher | Rockefeller University Press (United States) |
| Publisher Date | 1998-04-20 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Arabidopsis Proteins Chloroplasts Genetics Gene Expression Regulation, Plant Physiology Intracellular Membranes Membrane Proteins Plant Proteins Zea Mays Amino Acid Sequence Chloroplast Proteins Ultrastructure Cloning, Molecular Gene Dosage Genes, Plant Molecular Sequence Data Mutation Phenotype Polyribosomes Chemistry RNA, Messenger RNA, Plant RNA, Ribosomal, 16S Sequence Analysis, DNA Sequence Homology, Amino Acid Research Support, U.S. Gov't, P.H.S. Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine |
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