TY - JOUR TI - Quantification and removal of some contaminating gases from acetylene used to study gas-utilizing enzymes and microorganisms. T2 - Applied and environmental microbiology DA - 1987/2/1/ PY - 1987/2/1/ UR - https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/16347278/?tool=EBI ER - TY - JOUR TI - Translational repression: Biological activity of plasmid-encoded bacteriophage T4 RegA protein AU - Miller, Eric S. AU - Karam, Jim AU - Dawson, Myra AU - Trojanowska, Maria AU - Gauss, Peter AU - Gold, Larry T2 - Journal of Molecular Biology AB - The RegA protein of bacteriophage T4 is a translational repressor that regulates expression of several phage early mRNAs. We have cloned wild-type and mutant alleles of the T4 regA gene under control of the heat-inducible, plasmid-borne leftward promoter (PL) of phage lambda. Expression of the cloned regA+ gene resulted in the synthesis of a protein that closely resembled phage-encoded RegA protein in biological properties. It repressed its own synthesis (autogenous translational control) as well as the synthesis of specific T4-encoded proteins that are known from other studies to be under RegA-mediated translational control. Cloned mutant alleles of regA exhibited derepressed synthesis of the mutant regA gene products and were ineffective in trans against RegA-sensitive mRNA targets. The effects of plasmid-encoded RegA proteins were also demonstrated in experiments using two compatible plasmids in uninfected Escherichia coli. The two-plasmid assays confirm the sensitivities of several cloned T4 genes to RegA-mediated translational repression and are well-suited for genetic analysis of RegA target sites. Repression specificity in this system was demonstrated by using wild-type and operator-constitutive translational initiation sites of T4 rIIB fused to lacZ. The results show that no additional T4 products are required for RegA-mediated translational repression. Additional evidence is provided for the proposal that uridine-rich mRNA sequences are preferred targets for the repressor. Surprisingly, plasmid-generated RegA protein represses the synthesis of some E. coli proteins and appears to enhance selectively the synthesis of others. The RegA protein may have multiple functions, and its binding sites are not restricted to phage mRNAs. DA - 1987/4// PY - 1987/4// DO - 10.1016/0022-2836(87)90670-x VL - 194 IS - 3 SP - 397-410 J2 - Journal of Molecular Biology LA - en OP - SN - 0022-2836 UR - http://dx.doi.org/10.1016/0022-2836(87)90670-x DB - Crossref ER - TY - JOUR TI - Chloroplast promoters AU - Hanley-Bowdoin, Linda AU - Chua, Nam-Hai T2 - Trends in Biochemical Sciences AB - DNA sequences required for accurate initiation of chloroplast transcription have been characterized in higher plants using chloroplast in vitro transcription systems. Although chloroplast promoters resemble bacterial promoters, they also have some unique properties. DA - 1987/1// PY - 1987/1// DO - 10.1016/0968-0004(87)90033-8 VL - 12 SP - 67-70 J2 - Trends in Biochemical Sciences LA - en OP - SN - 0968-0004 UR - http://dx.doi.org/10.1016/0968-0004(87)90033-8 DB - Crossref ER - TY - JOUR TI - Structure and variation in ribosomal RNA genes of pea: Characterization of a cloned rDNA repeat and chromosomal rDNA variants AU - Jorgensen, R.A. AU - Cuellar, R.E. AU - Thompson, W.F. T2 - Plant Molecular Biology DA - 1987/// PY - 1987/// DO - 10.1007/bf00016429 VL - 8 IS - 1 SP - 3–12 ER - TY - JOUR TI - A phytochrome-regulated transcript encodes ferredoxin in Pisum sativum AU - Dobres, M.S. AU - Elliot, R.C. AU - Watson, J.C. AU - Thompson, W.F. T2 - Plant Molecular Biology DA - 1987/// PY - 1987/// DO - 10.1007/bf00016434 VL - 8 SP - 53–59 ER - TY - JOUR TI - Developmental regulation of cytosine methylation in the nuclear ribosomal RNA genes of Pisum sativum AU - Watson, John C. AU - Kaufman, Lon S. AU - Thompson, William F. T2 - Journal of Molecular Biology AB - Prominent features of the cytosine methylation pattern of the Pisum sativum nuclear ribosomal RNA genes have been defined. Cytosine methylation within the C-C-G-G sequence was studied using the restriction enzymes HpaII and MspI and gel blot hybridizations of the restriction digests. The extent to which particular features of the methylation pattern change during seedling development has also been determined. Total cellular DNA, purified from defined sections of pea seedlings grown under different lighting conditions, was analyzed with DNA hybridization probes derived from different portions of a cloned member of the nuclear rRNA gene family. By use of an indirect end-labeling technique, a map of 23 cleavable HpaII and/or MspI sites in genomic rDNA was constructed. The map covers about 90% of the rDNA repeat including the entire non-transcribed spacer region and most of the rRNA coding sequences. One notable feature of the map is that the most prominent HpaII site, located about 800 base-pairs upstream from the 5′ end of the mature 18 S rRNA, is cleaved only in one of the two most abundant rDNA length variants (the short variant). With a gel blot assay specific for cleavage at this site, we estimated the HpaII sensitivity of DNA preparations from several stages of pea seedling development. We find that, while methylation is generally low in young seedlings, DNA obtained from the apical buds of pea seedlings is highly methylated. Further, the methylation level of rDNA within the pea bud decreases as the buds are allowed to develop under continuous white light. Our data, taken together with published studies on pea seedling development, indicate that cytosine methylation levels may be related to the regulated expression of the nuclear rRNA genes in pea. DA - 1987/1// PY - 1987/1// DO - 10.1016/0022-2836(87)90622-x VL - 193 IS - 1 SP - 15-26 J2 - Journal of Molecular Biology LA - en OP - SN - 0022-2836 UR - http://dx.doi.org/10.1016/0022-2836(87)90622-x DB - Crossref ER - TY - JOUR TI - Specific mRNA and rRNA Levels in Greening Pea Leaves during Recovery from Iron Stress AU - Spiller, S. C. AU - Kaufman, L. S. AU - Thompson, W. F. AU - Briggs, W. R. T2 - PLANT PHYSIOLOGY AB - Hydroponically grown pea seedlings (Pisum sativum L., cv Alaska) were subjected to Fe stress for 10 to 16 days to produce mature chlorotic leaves. Greening was initiated by adding Fe to the nutrient solution. The levels of chlorophylls, chloroplast, and cytoplasmic rRNAs, and specific chloroplast- and nucleus-encoded mRNAs were all significantly lower in leaves developing during iron stress than in nonstressed leaves. In plants greening after addition of Fe, nuclear transcripts encoding chlorophyll a/b-binding protein and the small subunit of ribulose bisphosphate carboxylase/oxygenase increased about 5-fold in abundance following an 18 to 24 hour lag, as did the chloroplast-encoded transcript for the large subunit of the carboxylase/oxygenase. Chloroplast rRNA showed an increase over that in continually stressed control leaves only after a 40 hour lag. The chloroplast-encoded transcript encoding the Q(B)-binding 32 kilodalton polypeptide of Photosystem II showed little change during greening. Chlorophyll itself increased gradually after a lag period of 24 hours, with an increase in chlorophyll a slightly preceding that of chlorophyll b. Kinetic considerations suggest that the changes observed represent a coordinate series of events initiated by readdition of Fe and occurring in parallel. Though accumulation of mRNA for light-harvesting, chlorophyll-a/b-binding protein might limit chlorophyll accumulation at the onset, subsequent changes in the mRNA do not parallel chlorophyll changes. All three of the mRNAs showing recovery on addition of Fe to Fe-stressed plants undergo sharp diurnal fluctuations in abundance. Such fluctuations are comparable to those in nonstressed controls (mRNA for light-harvesting protein) or considerably more pronounced (mRNAs for carboxylase large and small subunits). The carboxylase small subunit mRNA and that for light-harvesting chlorophyll-binding protein were measured under constant conditions of light and temperature. Though a rhythm in greening leaves was hard to detect, it was prominent in the Fe-sufficient controls, persisting undamped through three full cycles for both mRNAs, and hence is probably circadian. DA - 1987/6/1/ PY - 1987/6/1/ DO - 10.1104/pp.84.2.409 VL - 84 IS - 2 SP - 409-414 J2 - PLANT PHYSIOLOGY LA - en OP - SN - 0032-0889 1532-2548 UR - http://dx.doi.org/10.1104/pp.84.2.409 DB - Crossref ER - TY - JOUR TI - Chloroplast DNA evolution among legumes: Loss of a large inverted repeat occurred prior to other sequence rearrangements AU - Palmer, Jeffrey D. AU - Osorio, Bernardita AU - Aldrich, Jane AU - Thompson, William F. T2 - Current Genetics AB - We have compared the sequence organization of four previously uncharacterized legume chloroplast DNAs - from alfalfa, lupine, wisteria and subclover — to that of legume chloroplast DNAs that either retain a large, ribosomal RNA-encoding inverted repeat (mung bean) or have deleted one half of this repeat (broad bean). The circular, 126 kilobase pair (kb) alfalfa chloroplast genome, like those of broad bean and pea, lacks any detectable repeated sequences and contains only a single set of ribosomal RNA genes. However, in contrast to broad bean and pea, alfalfa chloroplast DNA is unrearranged (except for the deletion of one segment of the inverted repeat) relative to chloroplast DNA from mung bean. Together with other findings reported here, these results allow us to determine which of the four possible inverted repeat configurations was deleted in the alfalfa-pea-broad bean lineage, and to show how the present-day broad bean genome may have been derived from an alfalfa-like ancestral genome by two major sequence inversions. The 147 kb lupine chloroplast genome contains a 22 kb inverted repeat and has essentially complete colinearity with the mung bean genome. In contrast, the 130 kb wisteria genome has deleted one half of the inverted repeat and appears colinear with the alfalfa genome. The 140 kb subclover genome has been extensively rearranged and contains a family of at least five dispersed repetitive sequence elements, each several hundred by in size; this is the first report of dispersed repeats of this size in a land plant chloroplast genome. We conclude that the inverted repeat has been lost only once among legumes and that this loss occurred prior to all the other rearrangements observed in subclover, broad bean and pea. Of those lineages that lack the inverted repeat, some are stable and unrearranged, other have undergone a moderate amount of rearrangement, while still others have sustained a complex series of rearrangement either with or without major sequence duplications and transpositions. DA - 1987/1// PY - 1987/1// DO - 10.1007/bf00355401 VL - 11 IS - 4 SP - 275-286 J2 - Curr Genet LA - en OP - SN - 0172-8083 1432-0983 UR - http://dx.doi.org/10.1007/bf00355401 DB - Crossref ER - TY - JOUR TI - Light-regulated changes in DNase I hypersensitive sites in the rRNA genes of Pisum sativum AU - Kaufman, L. S. AU - Watson, J. C. AU - Thompson, W. F. T2 - Proceedings of the National Academy of Sciences AB - We have examined the rDNA chromatin of Pisum sativum plants grown with or without exposure to light for the presence of DNase I hypersensitive sites and possible developmental changes in their distribution. Isolated nuclei from pea seedlings were incubated with various concentrations of DNase I. To visualize the hypersensitive sites, DNA purified from these nuclei was restricted and analyzed by gel blot hybridization. We find that several sites exist in both the coding and noncoding regions of rDNA repeating units. Several of the sites in the nontranscribed spacer region are present in the light but are absent in the dark. Conversely, the hypersensitive sites within the mature rRNA coding regions are present in the dark but absent in the light. There are two major length variants of the rRNA genes in P. sativum var. Alaska. The sites in the nontranscribed spacer region that appear during the light treatment occur only in the shorter of these two length variants in this cultivar. DA - 1987/3/1/ PY - 1987/3/1/ DO - 10.1073/pnas.84.6.1550 VL - 84 IS - 6 SP - 1550-1554 J2 - Proceedings of the National Academy of Sciences LA - en OP - SN - 0027-8424 1091-6490 UR - http://dx.doi.org/10.1073/pnas.84.6.1550 DB - Crossref ER - TY - JOUR TI - Acetylene is an active-site-directed, slow-binding, reversible inhibitor of Azotobacter vinelandii hydrogenase AU - Hyman, Michael R. AU - Arp, Daniel J. T2 - Biochemistry AB - ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTAcetylene is an active-site-directed, slow-binding, reversible inhibitor of Azotobacter vinelandii hydrogenaseMichael R. Hyman and Daniel J. ArpCite this: Biochemistry 1987, 26, 20, 6447–6454Publication Date (Print):October 1, 1987Publication History Published online1 May 2002Published inissue 1 October 1987https://doi.org/10.1021/bi00394a023RIGHTS & PERMISSIONSArticle Views76Altmetric-Citations19LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InReddit PDF (1011 KB) Get e-Alerts Get e-Alerts DA - 1987/10/1/ PY - 1987/10/1/ DO - 10.1021/bi00394a023 VL - 26 IS - 20 SP - 6447-6454 J2 - Biochemistry SN - 0006-2960 UR - https://doi.org/10.1021/bi00394a023 DB - ACS Publications Y2 - 2019/2/1/ ER - TY - JOUR TI - Quantification and removal of some contaminating gases from acetylene used to study gas-utilizing enzymes and microorganisms AU - Hyman, M. R. AU - Arp, D. J. T2 - Applied and Environmental Microbiology C2 - PMC203655 DA - 1987/2// PY - 1987/2// VL - 53 IS - 2 SP - 298-303 J2 - Appl. Environ. Microbiol. LA - eng SN - 0099-2240 DB - PubMed ER - TY - JOUR TI - System and synopsis of Cornus subgen. Syncarpea (Nakai) Q. Y. Xiang (Cornaceae) AU - Xiang, Q.Y. T2 - Bulletin of Botanical Research DA - 1987/// PY - 1987/// VL - 7 IS - 2 SP - 33–52 ER - TY - JOUR TI - Cytological studies on some plants of Sichuan and its neighboring regions (I). AU - Tang, Y.C. AU - Xiang, Q.Y. AU - Cao, Y.L. T2 - Acta Phytotax. Sin DA - 1987/// PY - 1987/// VL - 22 SP - 343–350 ER - TY - JOUR TI - Cytological studies on some plants of East China (I) AU - Tang, Y.C. AU - Xiang, Q.Y. T2 - Acta Phytotax. Sin. DA - 1987/// PY - 1987/// VL - 25 SP - 1–8 ER - TY - JOUR TI - A neglected character of Cornus L. s. l. with special reference to a new subgenus -- Sinocornus AU - Xiang, Q.Y. T2 - Acta Phytotax. Sin. DA - 1987/// PY - 1987/// VL - 25 SP - 25–131 ER - TY - JOUR TI - Divergence of Methanogens, Conservation of the His I Gene Sequence in all Three Biological Kingdoms and the Status of Methanobacterium Thermoautotrophicum AU - Reeve, John N. AU - Beckler, Gregory S. AU - Brown, James W. AU - Cram, David S. AU - Haas, Elizabeth S. AU - Hamilton, Paul T. AU - Morris, Christina J. AU - Sherf, Bruce A. AU - Weil, Clifford F. T2 - Microbial Growth on C1 Compounds AB - Methanogens are archaebacteria [1]. It was therefore somewhat surprising when it was shown that methanogen-derived genes could function in eubacterial species [2]. This has offered the opportunity of using gene cloning in Escherichia coli to investigate the basic structure of methanogen genes [3, 4] and to use E. coli to synthesize methanogen enzymes involved in methanogenesis [5] and nitrogen fixation [6]. DA - 1987/// PY - 1987/// DO - 10.1007/978-94-009-3539-6_31 SP - 255-260 ER -