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  • 1
    Electronic Resource
    Electronic Resource
    Auxin-induced changes in the level of translatable ribosomal protein messenger ribonucleic acids in soybean hypocotyl (1983)
    s.l. : American Chemical Society
    Biochemistry 22 (1983), S. 4131-4139 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00286a022
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  • 2
    Electronic Resource
    Electronic Resource
    Control of nitrogen and carbon metabolism in root nodules (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 85 (1992), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Because legume root nodules have high rates of carbon and nitrogen metabolism, they are ideal for the study of plant physiology, biochemistry and molecular biology. Many plant enzymes involved in carbon and nitrogen assimilation have enhanced activity and enzyme protein in nodules as compared to other plant organs. For all intents and purposes the interior of the root nodule is O2 limited. Both plant and bacterial components of effective root nodules have unique adaptive features for maximizing carbon and nitrogen metabolism in an O2-limited environment. Plant glycolysis appears to be shunted to malic acid synthesis with further reductive synthesis to fumarate and succinate. Nodule bacteroids utilize these organic acids for the energy to fuel nitrogenase activity. Activities of the plant enzymes phosphoenolpyruvate carboxylase (PEPC, EC 4.1.1.31), malate dehydrogenase (MDH, EC 1.1.1.37) and aspartate aminotransferase (AAT, EC 2.6.1.1), which are very high in nodules, may mediate the flux of carbon between organic and amino acid pools. Dark CO2 fixation via nodule PEPC can provide up to 25% of the carbon needed for malate and aspartate synthesis. At least three of the plant proteins showing enhanced expression in root nodules are O2 regulated. Isolation of alfalfa cDNAs encoding PEPC, AAT, NADH-glutamate synthase (NADH-GOGAT, EC 1.4.1.14) and aldolase (EC 4.1.2.13) will offer new tools to assess molecular events controlling nodule carbon and nitrogen metabolism.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1992.tb04731.x
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  • 3
    Electronic Resource
    Electronic Resource
    Subnuclear distribution of the entire complement of linker histone variants in Arabidopsis thaliana (1999)
    Springer
    Chromosoma 108 (1999), S. 345-355 
    Details
    ISSN: 1432-0886
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Linker histones (e.g. H1, H5, H1°) are thought to exert control on chromatin function by restricting nucleosomal dynamics. All higher eukaryotes possess a diverse family of linker histones, which may exhibit functional specialization. Arabidopsis thaliana apparently contains a minimal complement of linker histone structural variants and therefore is an ideal model for investigating functional differentiation among linker histones. Histones H1-1 and H1-2 are relatively similar proteins that are expressed in a wide variety of tissues and make up the majority of linker histone while H1-3 is a highly divergent minor variant protein that is induced by drought stress. We are interested in determining whether the in vivo distribution of each of these proteins also differs. To this end, we have produced subtype-specific antibodies and have localized each of the three proteins at the intranuclear and DNA sequence levels by indirect immunofluorescence and immunoprecipitation, respectively. Antibodies against linker histones H1-1 and H1-2 decorate nuclei in patterns very similar to 4’,6-diamidino-2-phenylindole (DAPI) staining, but different than the staining pattern of total histones. In contrast, antibodies made against two regions of H1-3 bind to chromatin in a diffuse pattern distinct from the DAPI-staining pattern. We also describe a technique to determine the localization of plant linker histone variants along regions of chromatin, employing in vivo chemical DNA-protein cross-linking to preserve native associations followed by immunoprecipitation with subtype-specific antibodies. We use this technique to demonstrate that, in contrast to the major linker histones, H1-3 does not bind the repetitive sequences pAL1 and 5S rDNA. In addition, we show that linker histones are bound to the compacted nucleosomal arrays at the telomere but with reduced stoichiometry. Taken together, our results suggest that plants, as has been shown for animals, possess a variant linker histone that is differentially localized.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004120050386
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  • 4
    Electronic Resource
    Electronic Resource
    Differential expression of six glutamine synthetase genes in Zea mays (1993)
    Springer
    Plant molecular biology 23 (1993), S. 401-407 
    Details
    ISSN: 1573-5028
    Keywords: gene-specific probes ; glutamine synthetase ; transcript accumulation ; Zea mays
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The maize genome has been shown to contain six glutamine synthetase (GS) genes with at least four different expression patterns. Noncoding 3′ gene-specific probes were constructed from all six GS cDNA clones and used to examine transcript levels in selected organs by RNA gel blot hybridization experiments. The transcript of the single putative chloroplastic GS2 gene was found to accumulate primarily in green tissues, whereas the transcripts of the five putative GS1 genes were shown to accumulate preferentially in roots. The specific patterns of transcript accumulation were quite distinct for the five GS1 genes, with the exception of two closely related genes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00029015
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  • 5
    Electronic Resource
    Electronic Resource
    Chlamydomonas transcripts encoding three divergent plastid chaperonins are heat-inducible (1995)
    Springer
    Plant molecular biology 27 (1995), S. 1031-1035 
    Details
    ISSN: 1573-5028
    Keywords: Chlamydomonas reinhardtii ; chaperonin ; cpn60 ; chaperone ; heat shock
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Three cDNAs encoding plastid cpn60 chaperonin subunits have been isolated from the unicellular green alga Chlamydomonas reinhardtii. Based on comparisons of the predicted amino acid sequences, we conclude that Chlamydomonas, like higher plants, contains divergent plastid cpn60-α and cpn60-β subunits. The predicted amino acid sequences of the two Chlamydomonas cpn60-β subunits differ significantly (24% divergent), indicating that the two cpn60-β subunits have been selectively maintained for a considerable period of time. Unlike plastid chaperonin trnascripts in higher plants, heat shock conditions (42°C) lead to a rapid increase (10-to 30-fold) in the level of each of the three plastid transcripts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00037029
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  • 6
    Electronic Resource
    Electronic Resource
    Characterization of rps17, rpl9 and rpl15: three nucleus-encoded plastid ribosomal protein genes (1992)
    Springer
    Plant molecular biology 18 (1992), S. 931-944 
    Details
    ISSN: 1573-5028
    Keywords: Arabidopsis thaliana ; chloroplast ; differential gene expression ; gene structure ; ribosomal protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Approximately two-thirds of the 55 to 60 plastid ribosomal proteins are encoded in the nucleus. Since the protein products of each of these genes are needed in equal amounts for ribosome assembly, their expression may be coordinately regulated by common mechanisms. To begin to understand how the expression of these genes is regulated, we have isolated cDNA and genomic clones for three plastid ribosomal protein genes from an Arabidopsis thaliana library. The genes rps17, rpl9 and rpl15, encoding plastid ribosomal proteins CS17, CL9 and CL15, respectively, are located in the nuclear genome and Southern blot data suggest that each is a single copy gene in A. thaliana. Northern blot data show that transcripts from rps17, rpl9 and rpl15 are much more abundant in leaves and stems than they are in roots. The nucleotide sequences of each of these three genes were determined and their transcriptional initiation sites identified. rps17 transcripts have multiple 5′ ends suggesting that they are initiated at multiple sites or are post-transcriptionally processed at their 5′ end. rpl9 and rpl15 apparently have unique transcriptional initiation sites but are post-transcriptionally processed to remove six and three introns, respectively, from their primary transcripts. We have examined the genomic sequences for motifs that may be important for the proper expression of these genes. A 7 bp sequence motif, whose consensus is 5′-AGGCCCA-3′, flanked by AT-rich regions was identified between 38 and 73 nucleotides upstream of the rps17, rpl9 and rpl15 transcriptional initiation sites.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00019207
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  • 7
    Electronic Resource
    Electronic Resource
    Alfalfa root nodule phosphoenolpyruvate carboxylase: characterization of the cDNA and expression in effective and plant-controlled ineffective nodules (1992)
    Springer
    Plant molecular biology 20 (1992), S. 437-450 
    Details
    ISSN: 1573-5028
    Keywords: alfalfa ; gene regulation ; nodulin ; phosphoenolpyruvate carboxylase ; root nodule development
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Phosphoenolpyruvate carboxylase (PEPC) plays a key role in N2 fixation and ammonia assimilation in legume root nodules. The enzyme can comprise up to 2% of the soluble protein in root nodules. We report here the isolation and characterization of a cDNA encoding the nodule-enhanced form of PEPC. Initially, a 2945 bp partial-length cDNA was selected by screening an effective alfalfa nodule cDNA library with antibodies prepared against root nodule PEPC. The nucleotide sequence encoding the N-terminal region of the protein was obtained by primer-extension cDNA synthesis and PCR amplification. The complete amino acid sequence of alfalfa PEPC was deduced from these cDNA sequences and shown to bear striking similarity to other plant PEPCs. Southern blots of alfalfa genomic DNA indicate that nodule PEPC is a member of a small gene family. During the development of effective root nodules, nodule PEPC activity increases to a level that is 10- to 15-fold greater than that in root and leaf tissue. This increase appears to be the result of increases in amount of enzyme protein and PEPC mRNA. Ineffective nodules have substantially less PEPC mRNA, enzyme protein and activity than do effective nodules. Maximum expression of root nodule PEPC appears to be related to two signals. The first signal is associated with nodule initiation while the second signal is associated with nodule effectiveness. Regulation of root nodule PEPC activity may also involve post-translational processes affecting enzyme activity and/or degradation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00040603
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  • 8
    Electronic Resource
    Electronic Resource
    A drought-stress-inducible histone gene in Arabidopsis thaliana is a member of a distinct class of plant linker histone variants (1997)
    Springer
    Plant molecular biology 34 (1997), S. 629-641 
    Details
    ISSN: 1573-5028
    Keywords: linker histone variants ; gene family ; environmental stress ; chromatin ; Arabidopsis ; abscisic acid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have isolated and characterized a gene, His1-3, encoding a structurally divergent linker histone in Arabidopsis thaliana. Southern and northern hybridization data indicate that A. thaliana expresses three single-copy linker histone genes, each encoding a structurally distinct variant. H1-3 is a considerably smaller protein (167 amino acids with a mass of 19.0 kDa) than any other described linker histone from higher eukaryotes. We examined the expression of His1-3 at the RNA and protein levels and found that it is induced specifically by water stress. In contrast, expression of His1-1, His1-2 and His4 appear unaffected by water stress. Furthermore, the primary structure of the protein possesses distinct characteristics that are shared with another drought-inducible linker histone, H1-D, isolated from Lycopersicon pennellii. Based on structural characteristics of the deduced protein and its inducible expression, we hypothesize that H1-3 and H1-D are linker histone variants that have specialized roles in the structure and function of plant chromatin and therefore they can be considered to be members of a unique subclass of plant histones. Immunoblotting with an antibody produced against a short polypeptide in the conserved domain of this subtype indicates that similar proteins may exist in other plants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005886011722
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  • 9
    Electronic Resource
    Electronic Resource
    Isolation of nuclear encoded plastid ribosomal protein cDNAs (1986)
    Springer
    Molecular genetics and genomics 202 (1986), S. 186-193 
    Details
    ISSN: 1617-4623
    Keywords: Ribosomal proteins ; Chloroplast ; Protein transport
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A pea leaf cDNA library was constructed in the expression vector λgt11 and screened with antisera raised against proteins extracted from 30S and 50S ribosomal subunits and 70S ribosomes prepared from isolated pea chloroplasts. Six recombinant phage were identified that encoded fusion proteins containing plastid ribosomal protein antigenic determinants. Phage-induced cell lysate proteins, containing the fusion proteins, were bound to nitrocellulose membranes and used as affinity matrices to prepare monospecific antibodies. These antibodies were then used to identify by Western blotting which plastid ribosomal protein shared antigenic determinants with the fusion proteins. cDNA inserts from the antigen-producing phage were used to hybrid-select complementary mRNAs. The cell-free translation products of these mRNAs were added to a pea chloroplast in vitro transport system and imported proteins analyzed by two-dimensional gel electrophoresis. The imported proteins comigrated with the plastid ribosomal proteins that were identified as being antigenically related to the fusion proteins produced by the corresponding recombinant phage. The imported proteins were 3,500–5,500 daltons smaller than their precursors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00331635
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  • 10
    Electronic Resource
    Electronic Resource
    Molecular analysis of allelic polymorphism at the AAT2 locus of alfalfa (1993)
    Springer
    Molecular genetics and genomics 241 (1993), S. 124-128 
    Details
    ISSN: 1617-4623
    Keywords: Aspartate aminotransferase ; Alleles ; Alfalfa ; Nitrogen fixation ; Transit peptide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Aspartate aminotransferase (AAT) plays a key enzymatic role in the assimilation of symbiotically fixed nitrogen in legume root nodules. In alfalfa, two distinct genetic loci encode dimeric AAT enzymes: AAT1, which predominates in roots, and AAT2, which is expressed at high levels in nodules. Three allozymes of AAT2 (AAT2a, −2b and −2c), differing in net charge, result from the expression of two alleles, AAT2A and AAT2C, at this locus. Utilizing antiserum to alfalfa AAT2, we have previously isolated from an expression library one AAT2 cDNA clone. This clone was used as a hybridization probe to screen cDNA libraries for additional AAT2 cDNAs. Four different clones were obtained, two each that encode the AAT2a and AAT2c enyzme subunits. These two sets of cDNAs encode polypeptides that differ in net charge depending upon the amino acid at position 296 (valine or glutamic acid). Within each set of alleles, the two members differ from each other by the presence or absence of a 30 by (ten amino acid) sequence. The presence or absence of this ten amino acid sequence has no effect on the size or charge of the mature AAT2 protein because it is located within the region encoding the protein's transit peptide, which is proteolytically removed upon transport into plastids. The data suggest that a deletion event has occurred independently in two AAT2 progenitor alleles, resulting in the four allelic cDNA variants observed. The deletion of this ten amino acid sequence does not appear to impair the normal maturation of the enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00280209
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