Annual review of plant physiology and plant molecular biology最新文献

{"title":"Enzymes and other agents that enhance cell wall extensibility.","authors":"D. Cosgrove","doi":"10.1146/ANNUREV.ARPLANT.50.1.391","DOIUrl":"https://doi.org/10.1146/ANNUREV.ARPLANT.50.1.391","url":null,"abstract":"Polysaccharides and proteins are secreted to the inner surface of the growing cell wall, where they assemble into a network that is mechanically strong, yet remains extensible until the cells cease growth. This review focuses on the agents that directly or indirectly enhance the extensibility properties of growing walls. The properties of expansins, endoglucanases, and xyloglucan transglycosylases are reviewed and their postulated roles in modulating wall extensibility are evaluated. A summary model for wall extension is presented, in which expansin is a primary agent of wall extension, whereas endoglucanases, xyloglucan endotransglycosylase, and other enzymes that alter wall structure act secondarily to modulate expansin action.","PeriodicalId":80493,"journal":{"name":"Annual review of plant physiology and plant molecular biology","volume":"50 1","pages":"391-417"},"PeriodicalIF":0.0,"publicationDate":"1999-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/ANNUREV.ARPLANT.50.1.391","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"64258805","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":"MEIOTIC CHROMOSOME ORGANIZATION AND SEGREGATION IN PLANTS.","authors":"R. Kelly Dawe","doi":"10.1146/annurev.arplant.49.1.371","DOIUrl":"https://doi.org/10.1146/annurev.arplant.49.1.371","url":null,"abstract":"<p><p>During meiosis, homologous chromosomes are brought together to be recombined and segregated into separate haploid gametes. This requires two cell divisions, an elaborate prophase with five substages, and specialized mechanisms that regulate the association of sister chromatids. This review focuses on plant chromosomes and chromosome-associated structures, such as recombination nodules and kinetochores, that ensure accurate meiotic chromosome segregation.</p>","PeriodicalId":80493,"journal":{"name":"Annual review of plant physiology and plant molecular biology","volume":"49 ","pages":"371-395"},"PeriodicalIF":0.0,"publicationDate":"1998-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.arplant.49.1.371","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40834947","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":"SPLICE SITE SELECTION IN PLANT PRE-mRNA SPLICING.","authors":"J. W. S. Brown,&nbsp;C. G. Simpson","doi":"10.1146/annurev.arplant.49.1.77","DOIUrl":"https://doi.org/10.1146/annurev.arplant.49.1.77","url":null,"abstract":"<p><p>The purpose of this review is to highlight the unique and common features of splice site selection in plants compared with the better understood yeast and vertebrate systems. A key question in plant splicing is the role of AU sequences and how and at what stage they are involved in spliceosome assembly. Clearly, intronic U- or AU-rich and exonic GC- and AG-rich elements can influence splice site selection and splicing efficiency and are likely to bind proteins. It is becoming clear that splicing of a particular intron depends on a fine balance in the \"strength\" of the multiple intron signals involved in splice site selection. Individual introns contain varying strengths of signals and what is critical to splicing of one intron may be of less importance to the splicing of another. Thus, small changes to signals may severely disrupt splicing or have little or no effect depending on the overall sequence context of a specific intron/exon organization.</p>","PeriodicalId":80493,"journal":{"name":"Annual review of plant physiology and plant molecular biology","volume":"49 ","pages":"77-95"},"PeriodicalIF":0.0,"publicationDate":"1998-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.arplant.49.1.77","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40912782","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":"LESSONS FROM SEQUENCING OF THE GENOME OF A UNICELLULAR CYANOBACTERIUM, SYNECHOCYSTIS SP. PCC6803.","authors":"H. Kotani,&nbsp;S. Tabata","doi":"10.1146/annurev.arplant.49.1.151","DOIUrl":"https://doi.org/10.1146/annurev.arplant.49.1.151","url":null,"abstract":"<p><p>The nucleotide sequence of the entire genome of the unicellular cyanobacterium, Synechocystis sp. PCC6803, has been determined. The length of the circular genome was 3,573,480 bp, and a total of 3168 protein-coding genes were assigned to the genome by a computer-assisted analysis. The functions of approximately 45% of the genes were deduced based on sequence similarity to known genes. Here are distinctive features of genetic information carried by the cyanobacteria, which have a phylogenetic relationship to both bacteria and plants.</p>","PeriodicalId":80493,"journal":{"name":"Annual review of plant physiology and plant molecular biology","volume":"49 ","pages":"151-171"},"PeriodicalIF":0.0,"publicationDate":"1998-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.arplant.49.1.151","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40912785","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":"ABSCISIC ACID SIGNAL TRANSDUCTION.","authors":"Jeffrey Leung,&nbsp;Jerome Giraudat","doi":"10.1146/annurev.arplant.49.1.199","DOIUrl":"https://doi.org/10.1146/annurev.arplant.49.1.199","url":null,"abstract":"<p><p>The plant hormone abscisic acid (ABA) plays a major role in seed maturation and germination, as well as in adaptation to abiotic environmental stresses. ABA promotes stomatal closure by rapidly altering ion fluxes in guard cells. Other ABA actions involve modifications of gene expression, and the analysis of ABA-responsive promoters has revealed a diversity of potential cis-acting regulatory elements. The nature of the ABA receptor(s) remains unknown. In contrast, combined biophysical, genetic, and molecular approaches have led to considerable progress in the characterization of more downstream signaling elements. In particular, substantial evidence points to the importance of reversible protein phosphorylation and modifications of cytosolic calcium levels and pH as intermediates in ABA signal transduction. Exciting advances are being made in reassembling individual components into minimal ABA signaling cascades at the single-cell level.</p>","PeriodicalId":80493,"journal":{"name":"Annual review of plant physiology and plant molecular biology","volume":"49 ","pages":"199-222"},"PeriodicalIF":0.0,"publicationDate":"1998-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.arplant.49.1.199","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40912787","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 OVULE DEVELOPMENT.","authors":"C. S. Gasser,&nbsp;J. Broadhvest,&nbsp;B. A. Hauser","doi":"10.1146/annurev.arplant.49.1.1","DOIUrl":"https://doi.org/10.1146/annurev.arplant.49.1.1","url":null,"abstract":"<p><p>Ovules are the direct precursors of seeds and thus play central roles in sexual plant reproduction and human nutrition. Extensive classical studies have elucidated the evolutionary trends and developmental processes responsible for the current wide variety of ovule morphologies. Recently, ovules have been perceived as an attractive system for the study of genetic regulation of plant development. More than a dozen regulatory genes have now been identified through isolation of ovule mutants. Characterization of these mutants shows that some aspects of ovule development follow independent pathways, while other processes are interdependent. Some of these mutants have ovules resembling those of putative ancestors of angiosperms and may help in understanding plant evolution. Clones of several of the regulatory genes have been used to determine expression patterns and putative biochemical functions of the gene products. Newly constructed models of genetic regulation of ovule development provide a framework for interpretation of future discoveries.</p>","PeriodicalId":80493,"journal":{"name":"Annual review of plant physiology and plant molecular biology","volume":"49 ","pages":"1-24"},"PeriodicalIF":0.0,"publicationDate":"1998-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.arplant.49.1.1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40833986","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":"CALMODULIN AND CALMODULIN-BINDING PROTEINS IN PLANTS.","authors":"Raymond E. Zielinski","doi":"10.1146/annurev.arplant.49.1.697","DOIUrl":"https://doi.org/10.1146/annurev.arplant.49.1.697","url":null,"abstract":"<p><p>Calmodulin is a small Ca2+-binding protein that acts to transduce second messenger signals into a wide array of cellular responses. Plant calmodulins share many structural and functional features with their homologs from animals and yeast, but the expression of multiple protein isoforms appears to be a distinctive feature of higher plants. Calmodulin acts by binding to short peptide sequences within target proteins, thereby inducing structural changes, which alters their activities in response to changes in intracellular Ca2+ concentration. The spectrum of plant calmodulin-binding proteins shares some overlap with that found in animals, but a growing number of calmodulin-regulated proteins in plants appear to be unique. Ca2+-binding and enzymatic activation properties of calmodulin are discussed emphasizing the functional linkages between these processes and the diverse pathways that are dependent on Ca2+ signaling.</p>","PeriodicalId":80493,"journal":{"name":"Annual review of plant physiology and plant molecular biology","volume":"49 ","pages":"697-725"},"PeriodicalIF":0.0,"publicationDate":"1998-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.arplant.49.1.697","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40834327","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":"FROM VACUOLAR GS-X PUMPS TO MULTISPECIFIC ABC TRANSPORTERS.","authors":"Philip A. Rea,&nbsp;Ze-Sheng Li,&nbsp;Yu-Ping Lu,&nbsp;Yolanda M. Drozdowicz,&nbsp;Enrico Martinoia","doi":"10.1146/annurev.arplant.49.1.727","DOIUrl":"https://doi.org/10.1146/annurev.arplant.49.1.727","url":null,"abstract":"<p><p>While the concept of H+-coupling has dominated studies of energy-dependent organic solute transport in plants for over two decades, recent studies have demonstrated the existence of a group of organic solute transporters, belonging to the ATP-binding cassette (ABC) superfamily, that are directly energized by MgATP rather than by a transmembrane H+-electrochemical potential difference. Originally identified in microbial and animal cells, the ABC superfamily is one of the largest and most widespread protein families known. Competent in the transport of a broad range of substances including sugars, peptides, alkaloids, inorganic anions, and lipids, all ABC transporters are constituted of one or two copies each of an integral membrane sector and cytosolically oriented ATP-binding domain. To date, two major subclasses, the multidrug resistance-associated proteins (MRPs) and multidrug resistance proteins (MDRs) (so named because of the phenotypes conferred by their animal prototypes), have been identified molecularly in plants. However, only the MRPs have been defined functionally. This review therefore focuses on the functional capabilities, energetics, organization, and regulation of the plant MRPs. Otherwise known as GS-X pumps, or glutathione-conjugate or multispecific organic anion Mg2+-ATPases, the MRPs are considered to participate in the transport of exogenous and endogenous amphipathic anions and glutathionated compounds from the cytosol into the vacuole. Encoded by a multigene family and possessing a unique domain organization, the types of processes that likely converge and depend on plant MRPs include herbicide detoxification, cell pigmentation, the alleviation of oxidative damage, and the storage of antimicrobial compounds. Additional functional capabilities might include channel regulation or activity, and/or the transport of heavy metal chelates. The identification of the MRPs, in particular, and the demonstration of a central role for ABC transporters, in general, in plant function not only provide fresh insights into the molecular basis of energy-dependent solute transport but also offer the prospect for manipulating and investigating many fundamental processes that have hitherto evaded analysis at the transport level.</p>","PeriodicalId":80493,"journal":{"name":"Annual review of plant physiology and plant molecular biology","volume":"49 ","pages":"727-760"},"PeriodicalIF":0.0,"publicationDate":"1998-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.arplant.49.1.727","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40834328","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":"NUCLEAR CONTROL OF PLASTID AND MITOCHONDRIAL DEVELOPMENT IN HIGHER PLANTS.","authors":"P. Leon,&nbsp;A. Arroyo,&nbsp;S. Mackenzie","doi":"10.1146/annurev.arplant.49.1.453","DOIUrl":"https://doi.org/10.1146/annurev.arplant.49.1.453","url":null,"abstract":"<p><p>The nucleus must coordinate organelle biogenesis and function on a cell and tissue-specific basis throughout plant development. The vast majority of plastid and mitochondrial proteins and components involved in organelle biogenesis are encoded by nuclear genes. Molecular characterization of nuclear mutants has illuminated chloroplast development and function. Fewer mutants exist that affect mitochondria, but molecular and biochemical approaches have contributed to a greater understanding of this organelle. Similarities between organelles and prokaryotic regulatory molecules have been found, supporting the prokaryotic origin of chloroplasts and mitochondria. A striking characteristic for both mitochondria and chloroplast is that most regulation is posttranscriptional.</p>","PeriodicalId":80493,"journal":{"name":"Annual review of plant physiology and plant molecular biology","volume":"49 ","pages":"453-480"},"PeriodicalIF":0.0,"publicationDate":"1998-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.arplant.49.1.453","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40834950","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":"DNA METHYLATION IN PLANTS.","authors":"E. J. Finnegan,&nbsp;R. K. Genger,&nbsp;W. J. Peacock,&nbsp;E. S. Dennis","doi":"10.1146/annurev.arplant.49.1.223","DOIUrl":"https://doi.org/10.1146/annurev.arplant.49.1.223","url":null,"abstract":"<p><p>Methylation of cytosine residues in DNA provides a mechanism of gene control. There are two classes of methyltransferase in Arabidopsis; one has a carboxy-terminal methyltransferase domain fused to an amino-terminal regulatory domain and is similar to mammalian methyltransferases. The second class apparently lacks an amino-terminal domain and is less well conserved. Methylcytosine can occur at any cytosine residue, but it is likely that clonal transmission of methylation patterns only occurs for cytosines in strand-symmetrical sequences CpG and CpNpG. In plants, as in mammals, DNA methylation has dual roles in defense against invading DNA and transposable elements and in gene regulation. Although originally reported as having no phenotypic consequence, reduced DNA methylation disrupts normal plant development.</p>","PeriodicalId":80493,"journal":{"name":"Annual review of plant physiology and plant molecular biology","volume":"49 ","pages":"223-247"},"PeriodicalIF":0.0,"publicationDate":"1998-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.arplant.49.1.223","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40912788","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}