A5021631237- Photosynthetic Processes and Mechanisms
- Plant Stress Responses and Tolerance
- Plant Molecular Biology Research
- Genomics and Phylogenetic Studies
- Protist diversity and phylogeny
- Plant Diversity and Evolution
- Plant nutrient uptake and metabolism
- Antioxidant Activity and Oxidative Stress
- Light effects on plants
- Plant biochemistry and biosynthesis
- Microbial Community Ecology and Physiology
- Enzyme-mediated dye degradation
- Pesticide and Herbicide Environmental Studies
- Metal-Catalyzed Oxygenation Mechanisms
Michigan State University
2003-2020
Chloroplast division in plant cells is orchestrated by a complex macromolecular machine with components positioned on both the inner and outer envelope surfaces. The only plastid proteins identified to date are of endosymbiotic origin localized inside organelle. Employing positional cloning methods Arabidopsis conjunction novel strategy for pinpointing mutant locus, we have gene encoding new chloroplast protein, ARC5. Mutants ARC5 exhibit defects constriction, enlarged, dumbbell-shaped...
Summary The Arabidopsis arc1 ( accumulation and replication of chloroplasts 1 ) mutant has pale seedlings smaller, more numerous than the wild type. Previous work suggested that affects timing chloroplast division but does not function directly in process. We isolated ARC1 by map‐based cloning discovered it encodes FtsHi1 (At4g23940), one several FtsHi proteins Arabidopsis. These poorly studied resemble FtsH metalloproteases important for organelle biogenesis protein quality control are...
Chloroplast division is initiated by assembly of a mid-chloroplast FtsZ (Z) ring comprising two cytoskeletal proteins, FtsZ1 and FtsZ2. The division-site regulators ACCUMULATION AND REPLICATION OF CHLOROPLASTS3 (ARC3), MinD1, MinE1 restrict to the mid-plastid, but their roles are poorly understood. Using genetic analyses in Arabidopsis thaliana, we show that ARC3 mediates placement inhibiting Z-ring assembly, MinD1 function through ARC3. ftsZ1 null mutants exhibited some mid-plastid FtsZ2...
In plants, chloroplast division FtsZ proteins have diverged into two families, FtsZ1 and FtsZ2. is more divergent from its bacterial counterparts lacks a C-terminal motif conserved in most other FtsZs. To begin investigating structure-function relationships, we first identified T-DNA insertion mutation the single gene Arabidopsis thaliana, AtFtsZ1-1. Homozygotes null for FtsZ1, though impaired division, could be isolated set seed normally, indicating that not essential viability. We then...
FtsZ1 and FtsZ2 are phylogenetically distinct homologues of the tubulin-like bacterial cell division protein FtsZ that play major roles in initiation progression plastid plant cells. Both proteins components a mid-plastid ring, Z-ring, which functions as contractile ring on stromal surface chloroplast IEM (inner envelope membrane). have been shown to interact, but their vivo biochemical properties largely unknown. To gain insight into relationship between FtsZ2, present study we investigated...
1-Aminocyclopropane-1-carboxylic acid (ACC) oxidase (ACCO) catalyses the final step in ethylene biosynthesis converting ACC to ethylene, cyanide, CO2, dehydroascorbate and water with inputs of Fe(II), ascorbate, bicarbonate (as activators) oxygen. Cyanide activates ACCO. A 'nest' comprising several positively charged amino residues from C-terminal α-helix 11 along Lys158 Arg299 are proposed as binding sites for ascorbate coordinately activate ACCO reaction. The ACC, ascorbic Malus domestica...
Chloroplast size varies considerably in nature, but the underlying mechanisms are unknown. By exploiting a near-isogenic line population derived from cross between Arabidopsis (Arabidopsis thaliana) accessions Cape Verde Islands (Cvi-1), which has larger chloroplasts, and Landsberg erecta (Ler-0), with smaller we determined that large-chloroplast phenotype Cvi-1 is associated allelic variation gene encoding chloroplast-division protein FtsZ2-2, tubulin-related cytoskeletal component of...
Extended abstract of a paper presented at Microscopy and Microanalysis 2006 in Chicago, Illinois, USA, July 30 – August 3,