{"title":"NITRATE REDUCTASE STRUCTURE, FUNCTION AND REGULATION: Bridging the Gap between Biochemistry and Physiology.","authors":"Wilbur H. Campbell","doi":"10.1146/annurev.arplant.50.1.277","DOIUrl":"https://doi.org/10.1146/annurev.arplant.50.1.277","url":null,"abstract":"<p><p>Nitrate reductase (NR; EC 1.6.6.1-3) catalyzes NAD(P)H reduction of nitrate to nitrite. NR serves plants, algae, and fungi as a central point for integration of metabolism by governing flux of reduced nitrogen by several regulatory mechanisms. The NR monomer is composed of a ~100-kD polypeptide and one each of FAD, heme-iron, and molybdenum-molybdopterin (Mo-MPT). NR has eight sequence segments: (a) N-terminal \"acidic\" region; (b) Mo-MPT domain with nitrate-reducing active site; (c) interface domain; (d) Hinge 1 containing serine phosphorylated in reversible activity regulation with inhibition by 14-3-3 binding protein; (e) cytochrome b domain; (f) Hinge 2; (g) FAD domain; and (h) NAD(P)H domain. The cytochrome b reductase fragment contains the active site where NAD(P)H transfers electrons to FAD. A complete three-dimensional dimeric NR structure model was built from structures of sulfite oxidase and cytochrome b reductase. Key active site residues have been investigated. NR structure, function, and regulation are now becoming understood.</p>","PeriodicalId":80493,"journal":{"name":"Annual review of plant physiology and plant molecular biology","volume":" ","pages":"277-303"},"PeriodicalIF":0.0,"publicationDate":"1999-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.arplant.50.1.277","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40834034","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"PHOTOPROTECTION REVISITED: Genetic and Molecular Approaches.","authors":"Krishna K. Niyogi","doi":"10.1146/annurev.arplant.50.1.333","DOIUrl":"https://doi.org/10.1146/annurev.arplant.50.1.333","url":null,"abstract":"<p><p>The involvement of excited and highly reactive intermediates in oxygenic photosynthesis poses unique problems for algae and plants in terms of potential oxidative damage to the photosynthetic apparatus. Photoprotective processes prevent or minimize generation of oxidizing molecules, scavenge reactive oxygen species efficiently, and repair damage that inevitably occurs. This review summarizes several photoprotective mechanisms operating within chloroplasts of plants and green algae. The recent use of genetic and molecular biological approaches is providing new insights into photoprotection, especially with respect to thermal dissipation of excess absorbed light energy, alternative electron transport pathways, chloroplast antioxidant systems, and repair of photosystem II.</p>","PeriodicalId":80493,"journal":{"name":"Annual review of plant physiology and plant molecular biology","volume":" ","pages":"333-359"},"PeriodicalIF":0.0,"publicationDate":"1999-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.arplant.50.1.333","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40834036","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"THE 1-DEOXY-D-XYLULOSE-5-PHOSPHATE PATHWAY OF ISOPRENOID BIOSYNTHESIS IN PLANTS.","authors":"Hartmut K. Lichtenthaler","doi":"10.1146/annurev.arplant.50.1.47","DOIUrl":"https://doi.org/10.1146/annurev.arplant.50.1.47","url":null,"abstract":"<p><p>In plants the biosynthesis of prenyllipids and isoprenoids proceeds via two independent pathways: (a) the cytosolic classical acetate/mevalonate pathway for the biosynthesis of sterols, sesquiterpenes, triterpenoids; and (b) the alternative, non-mevalonate 1-deoxy-d-xylulose-5-phosphate (DOXP) pathway for the biosynthesis of plastidic isoprenoids, such as carotenoids, phytol (a side-chain of chlorophylls), plastoquinone-9, isoprene, mono-, and diterpenes. Both pathways form the active C5-unit isopentenyl diphosphate (IPP) as the precursor from which all other isoprenoids are formed via head-to-tail addition. This review summarizes current knowledge of the novel 1-deoxy-d-xylulose-5-phosphate (DOXP) pathway for isopentenyl diphosphate biosynthesis, apparently located in plastids. The DOXP pathway of IPP formation starts from D-glyceraldehyde-3-phosphate (GA-3-P) and pyruvate, with DOXP-synthase as the starting enzyme. This pathway provides new insight into the regulation of chloroplast metabolism.</p>","PeriodicalId":80493,"journal":{"name":"Annual review of plant physiology and plant molecular biology","volume":" ","pages":"47-65"},"PeriodicalIF":0.0,"publicationDate":"1999-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.arplant.50.1.47","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40834130","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Philippe Matile, Stefan Hortensteiner, Howard Thomas
{"title":"CHLOROPHYLL DEGRADATION.","authors":"Philippe Matile, Stefan Hortensteiner, Howard Thomas","doi":"10.1146/annurev.arplant.50.1.67","DOIUrl":"https://doi.org/10.1146/annurev.arplant.50.1.67","url":null,"abstract":"<p><p>Although the loss of green color in senescent leaves and ripening fruits is a spectacular natural phenomenon, research on chlorophyll breakdown has been largely neglected until recently. This review summarizes knowledge about the fate of chlorophyll in degreening tissues that has been gained during the past few years. Structures of end- and intermediary products of degradation as well as the biochemistry of the porphyrin-cleaving reaction have been elucidated. The intracellular localization of the catabolic pathway is particularly important in the regulation of chlorophyll breakdown. None of the genes encoding the related catabolic enzymes has so far been isolated, which makes chlorophyll degradation an area of opportunity for future research.</p>","PeriodicalId":80493,"journal":{"name":"Annual review of plant physiology and plant molecular biology","volume":" ","pages":"67-95"},"PeriodicalIF":0.0,"publicationDate":"1999-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.arplant.50.1.67","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40834131","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"CO2 CONCENTRATING MECHANISMS IN PHOTOSYNTHETIC MICROORGANISMS.","authors":"Aaron Kaplan, Leonora Reinhold","doi":"10.1146/annurev.arplant.50.1.539","DOIUrl":"https://doi.org/10.1146/annurev.arplant.50.1.539","url":null,"abstract":"<p><p>Many microorganisms possess inducible mechanisms that concentrate CO2 at the carboxylation site, compensating for the relatively low affinity of Rubisco for its substrate, and allowing acclimation to a wide range of CO2 concentrations. The organization of the carboxysomes in prokaryotes and of the pyrenoids in eukaryotes, and the presence of membrane mechanisms for inorganic carbon (Ci) transport, are central to the concentrating mechanism. The presence of multiple Ci transporting systems in cyanobacteria has been indicated. Certain genes involved in structural organization, Ci transport and the energization of the latter have been identified. Massive Ci fluxes associated with the CO2-concentrating mechanism have wide-reaching ecological and geochemical implications.</p>","PeriodicalId":80493,"journal":{"name":"Annual review of plant physiology and plant molecular biology","volume":" ","pages":"539-570"},"PeriodicalIF":0.0,"publicationDate":"1999-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.arplant.50.1.539","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40833980","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"GENETIC ANALYSIS OF HORMONE SIGNALING.","authors":"Peter McCourt","doi":"10.1146/annurev.arplant.50.1.219","DOIUrl":"https://doi.org/10.1146/annurev.arplant.50.1.219","url":null,"abstract":"<p><p>Phytohormones influence many diverse developmental processes ranging from seed germination to root, shoot, and flower formation. Recently, mutational analysis using the model plant Arabidopsis thaliana has been instrumental in determining the individual components of specific hormone signal transduction pathways. Moreover, epistasis and suppressor studies are beginning to explain how these genes and their products relate to one another. While no hormone transduction pathway is completely understood, the genes identified to date suggest that simple molecular rules can be established to explain how plant hormone signals are transduced. This review describes some of the shared characteristics of plant hormone signal transduction pathways and the properties for informational transfer common to many of the genes that specify the transduction of the signal.</p>","PeriodicalId":80493,"journal":{"name":"Annual review of plant physiology and plant molecular biology","volume":" ","pages":"219-243"},"PeriodicalIF":0.0,"publicationDate":"1999-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.arplant.50.1.219","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40834032","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"CELLULOSE BIOSYNTHESIS: Exciting Times for A Difficult Field of Study.","authors":"Deborah P. Delmer","doi":"10.1146/annurev.arplant.50.1.245","DOIUrl":"https://doi.org/10.1146/annurev.arplant.50.1.245","url":null,"abstract":"<p><p>The past few decades have witnessed exciting progress in studies on the biosynthesis of cellulose. In the bacterium Acetobacter xylinum, discovery of the activator of the cellulose synthase, cyclic diguanylic acid, opened the way for obtaining high rates of in vitro synthesis of cellulose. This, in turn, led to purification of the cellulose synthase and for the cloning of genes that encode the catalytic subunit and other proteins that bind the activator and regulate its synthesis and degradation, or that control secretion and crystallization of the microfibrils. In higher plants, a family of genes has been discovered that show interesting similarities and differences from the gene in bacteria that encodes the catalytic subunit of the synthase. Genetic evidence now supports the concept that members of this family encode the catalytic subunit in these organisms, with various members showing tissue-specific expression. Although the cellulose synthase has not yet been purified to homogeneity from plants, recent progress in this area suggests that this will soon be accomplished.</p>","PeriodicalId":80493,"journal":{"name":"Annual review of plant physiology and plant molecular biology","volume":" ","pages":"245-276"},"PeriodicalIF":0.0,"publicationDate":"1999-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.arplant.50.1.245","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40834033","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"PLANT PROTEIN SERINE/THREONINE KINASES: Classification and Functions.","authors":"D. G. Hardie","doi":"10.1146/annurev.arplant.50.1.97","DOIUrl":"https://doi.org/10.1146/annurev.arplant.50.1.97","url":null,"abstract":"<p><p>The first plant protein kinase sequences were reported as recently as 1989, but by mid-1998 there were more than 500, including 175 in Arabidopsis thaliana alone. Despite this impressive pace of discovery, progress in understanding the detailed functions of protein kinases in plants has been slower. Protein serine/threonine kinases from A. thaliana can be divided into around a dozen major groups based on their sequence relationships. For each of these groups, studies on animal and fungal homologs are briefly reviewed, and direct studies of their physiological functions in plants are then discussed in more detail. The network of protein-serine/threonine kinases in plant cells appears to act as a \"central processor unit\" (cpu), accepting input information from receptors that sense environmental conditions, phytohormones, and other external factors, and converting it into appropriate outputs such as changes in metabolism, gene expression, and cell growth and division.</p>","PeriodicalId":80493,"journal":{"name":"Annual review of plant physiology and plant molecular biology","volume":" ","pages":"97-131"},"PeriodicalIF":0.0,"publicationDate":"1999-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.arplant.50.1.97","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40834132","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"EDUCATOR AND EDITOR.","authors":"Martin Gibbs","doi":"10.1146/annurev.arplant.50.1.1","DOIUrl":"https://doi.org/10.1146/annurev.arplant.50.1.1","url":null,"abstract":"","PeriodicalId":80493,"journal":{"name":"Annual review of plant physiology and plant molecular biology","volume":" ","pages":"1-25"},"PeriodicalIF":0.0,"publicationDate":"1999-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.arplant.50.1.1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40834128","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"GAMETOPHYTE DEVELOPMENT IN FERNS.","authors":"Jo Ann Banks","doi":"10.1146/annurev.arplant.50.1.163","DOIUrl":"https://doi.org/10.1146/annurev.arplant.50.1.163","url":null,"abstract":"<p><p>The fern gametophyte has interested plant biologists for the past century because its structure and development is simple and amenable to investigation. Past studies have described many aspects of its development, including germination of the spore, patterns of cell division and differentiation, photomorphogenic or light-regulated responses, sex determination and differentiation of gametangia, hormone and pheromone responses, and fertilization. Several genes that are predicted to regulate some of these processes have been recently cloned, making it possible to analyze how these processes are controlled at a molecular level. The emergence of the fern Ceratopteris richardii as a model organism for readily identifying and characterizing mutations that affect key developmental processes in gametophytes makes it a powerful tool for dissecting the molecular mechanisms underlying these processes. If advances in gene cloning techniques and transformation are forthcoming in Ceratopteris, it is likely that the study of developmental processes in ferns will significantly contribute to our understanding of plant development and evolution beyond that which can be learned solely from studying angiosperms.</p>","PeriodicalId":80493,"journal":{"name":"Annual review of plant physiology and plant molecular biology","volume":" ","pages":"163-186"},"PeriodicalIF":0.0,"publicationDate":"1999-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.arplant.50.1.163","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40834134","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}