NDLI: Reciprocal Expression of Two Candidate Di-Iron Enzymes Affecting Photosystem I and Light-Harvesting Complex Accumulation

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Reciprocal Expression of Two Candidate Di-Iron Enzymes Affecting Photosystem I and Light-Harvesting Complex Accumulation

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Reciprocal Expression of Two Candidate Di-Iron Enzymes Affecting Photosystem I and Light-Harvesting Complex Accumulation

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Moseley, Jeffrey L. Page, M. Dudley Alder, Nancy P. Eriksson, Mats Quinn, Jeanette Soto, Feiris Theg, Steven M. Hippler, Michael Merchant, Sabeeha
Description	Country affiliation: United States Author Affiliation: Moseley JL ( Department of Chemistry and Biochemistry, University of California, Los Angeles, California 90095-1569, USA.)
Abstract	Crd1 (Copper response defect 1), which is required for the maintenance of photosystem I and its associated light-harvesting complexes in copper-deficient (-Cu) and oxygen-deficient (-O(2)) Chlamydomonas reinhardtii cells, is localized to the thylakoid membrane. A related protein, Cth1 (Copper target homolog 1), is shown to have a similar but not identical function by genetic suppressor analysis of gain-of-function sct1 (suppressor of copper target 1) strains that are transposon-containing alleles at CTH1. The pattern of Crd1 versus Cth1 accumulation is reciprocal; Crd1 abundance is increased in -Cu or -O(2) cells, whereas Cth1 accumulates in copper-sufficient (+Cu), oxygenated cells. This expression pattern is determined by a single trans-acting regulatory locus, CRR1 (COPPER RESPONSE REGULATOR 1), which activates transcription in -Cu cells. In +Cu cells, a 2.1-kb Cth1 mRNA is produced and translated, whereas Crd1 is transcribed only at basal levels, leading to Cth1 accumulation in +Cu cells. In -Cu cells, CRR1 function determines the activation of Crd1 expression and the production of an alternative 3.1-kb Cth1 mRNA that is extended at the 5' end relative to the 2.1-kb mRNA. Synthesis of the 3.1-kb mRNA, which encodes six small upstream open reading frames that possibly result in poor translation, blocks the downstream promoter through transcriptional occlusion. Fluorescence analysis of wild-type, crd1, and sct1 strains indicates that copper-responsive adjustment of the Cth1:Crd1 ratio results in modification of the interactions between photosystem I and associated light-harvesting complexes. The tightly coordinated CRR1-dependent regulation of isoenzymes Cth1 and Crd1 reinforces the notion that copper plays a specific role in the maintenance of chlorophyll proteins.
File Format	HTM / HTML
ISSN	10404651
e-ISSN	1531298X
Journal	THE PLANT CELL ONLINE
Issue Number	3
Volume Number	14
Language	English
Publisher	American Society of Plant Biologists
Publisher Date	2002-03-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Botany Algal Proteins Genetics Chlamydomonas Reinhardtii Oxidoreductases Photosynthesis Plant Proteins Metabolism Amino Acid Sequence Anaerobiosis Animals Drug Effects Copper Deficiency Copper Sulfate Pharmacology Dna Transposable Elements Expressed Sequence Tags Gene Expression Genotype Molecular Sequence Data Oxygen Peas Sequence Homology, Amino Acid Suppression, Genetic Thylakoids Comparative Study
Content Type	Text
Resource Type	Article
Subject	Cell Biology Plant Science

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