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841. Complex group-I introns in nuclear SSU rDNA of red and green algae: evidence of homing-endonuclease pseudogenes in the Bangiophyceae

Author:
Haugen, P.; Huss, V.A.R.; Nielsen, H.; Johansen, S.
Source:
Current genetics 1999 v.36 no.6 pp. 345-353
ISSN:
0172-8083
Subject:
protein secondary structure,   etc   ; pseudogenes; ribosomal RNA; open reading frames; catalytic activity; ribosomal DNA; Scenedesmus; amino acid sequences; ribosomal proteins; nucleases; introns; molecular conformation; Rhodophyta;     Show all 13 Subjects
DOI:
10.1007/s002940050509
PubMed:
10654088

842. DNA sequence analysis of the ribosomal DNA ITS2 region for the Anopheles punctulatus group of mosquitoes

Author:
Beebe, N.W.; Ellis, J.T.; Cooper, R.D.; Saul, A.
Source:
Insect molecular biology 1999 v.8 no.3 pp. 381-390
ISSN:
0962-1075
Subject:
protein secondary structure,   etc   ; guanosine; Anopheles koliensis; ribosomal DNA; phylogeny; cytosine; internal transcribed spacers; Anopheles farauti; DNA conformation; genetic variation; Anopheles punctulatus; Northern Territory; Solomon Islands; Papua New Guinea;     Show all 14 Subjects
Abstract:
... The internal transcribed spacer 2 (ITS2) from the ribosomal DNA was sequenced and characterized for ten cryptic species in the Anopheles punctulatus group, the members of which are major vectors of malaria and filariasis in the south-west Pacific. The length of the ITS2 ranged from 549 bp to 565 bp and displayed levels of sequence variation ranging from 2.3% to 24.3% due mainly to indels of simple ...
DOI:
10.1046/j.1365-2583.1999.83127.x
PubMed:
10469255

843. A novel group-II intron in the cox1 gene of the fission yeast Schizosaccharomyces pombe is inserted in the same codon as the mobile group-II intron aI2 in the Saccharomyces cerevisiae cox1 homologue. [Erratum: Jan 2000, v. 37 (1), p. 74.]

Author:
Schafer, B.; Wolf, K.
Source:
Current genetics 1999 v.35 no.6 pp. 602-608
ISSN:
0172-8083
Subject:
protein secondary structure,   etc   ; RNA-directed DNA polymerase; interspecific variation; mitochondrial DNA; Schizosaccharomyces pombe; mutation; Saccharomyces cerevisiae; codons; cytochrome-c oxidase; exons; nucleases; RNA; introns; molecular conformation;     Show all 14 Subjects
DOI:
10.1007/s002940050458

844. Compact organization of rRNA genes in the filamentous fungus Ashbya gossypii

Author:
Wendland, J.; Pohlmann, R.; Dietrich, F.; Steiner, S.; Mohr, C.; Philippsen, P.
Source:
Current genetics 1999 v.35 no.6 pp. 618-625
ISSN:
0172-8083
Subject:
protein secondary structure,   etc   ; interspecific variation; ribosomal RNA; RNA-binding proteins; ribosomal DNA; phylogeny; Saccharomyces cerevisiae; genes; plant pathogenic fungi; nucleotide sequences; molecular conformation;     Show all 11 Subjects
DOI:
10.1007/s002940050460
PubMed:
10467006

845. Comparison of ribosomal DNA ITS regions among geographic isolates of Cenococcum geophilum

Author:
Shinohara, M.L.; LoBuglio, K.F.; Rogers, S.O.
Source:
Current genetics 1999 v.35 no.5 pp. 527-535
ISSN:
0172-8083
Subject:
protein secondary structure,   etc   ; Cenococcum geophilum; restriction mapping; ribosomal DNA; geographical variation; phylogeny; strain differences; internal transcribed spacers; genetic variation; population; molecular conformation; Canada; Switzerland; Spain; Alaska; Finland;     Show all 16 Subjects
DOI:
10.1007/s002940050449
PubMed:
10369960

846. Purification and characterization of a lipoxygenase enzyme from durum wheat semolina

Author:
Barone, R.; Briante, R.; D'Auria, S.; Febbraio, F.; Vaccaro, C.; Del Giudice, L.; Borrelli, G.M.; Di Fonzo, N.; Nucci, R.
Source:
Journal of agricultural and food chemistry 1999 v.47 no.5 pp. 1924-1931
ISSN:
0021-8561
Subject:
protein secondary structure,   etc   ; linoleic acid; seeds; molecular weight; linoleate 13S-lipoxygenase; protein tertiary structure; beta-carotene; Triticum turgidum subsp. durum; pH; ionic strength; temperature; enzyme activity; molecular conformation;     Show all 13 Subjects
Abstract:
... Purification of a lipoxygenase enzyme from the cultivar Tresor of durum wheat semolina (Triticum turgidum var. durum Desf) was reinvestigated furnishing a new procedure. The 895-fold purified homogeneous enzyme showed a monomeric structure with a molecular mass of 95 +/- 5 kDa. Among the substrates tested, linoleic acid showed the highest k(cat)/K(m) value; a beta-carotene bleaching activity was a ...
DOI:
10.1021/jf980853z
PubMed:
10552472

847. A group-I intron in the mitochondrial small subunit ribosomal RNA gene of Sclerotinia sclerotiorum

Author:
Carbone, I.; Anderson, J.B.; Kohn, L.M.
Source:
Current genetics 1995 v.27 no.2 pp. 166-176
ISSN:
0172-8083
Subject:
protein secondary structure,   etc   ; Sclerotinia sclerotiorum; ribosomal RNA; open reading frames; mitochondrial DNA; ribosomal DNA; amino acid sequences; introns; molecular conformation;     Show all 9 Subjects
Abstract:
... A 1 380-bp intervening sequence within the mitochondrial small subunit ribosomal RNA (mt SSU rRNA) gene of the fungus Sclerotinia sclerotiorum has been sequenced and identified as a group-1 intron. This is the first report of an intron in the mt SSU rRNA gene. The intron shows close similarity in secondary structure to the subgroup-IC2 introns from Podospora (ND3i1, ND5i2, and COIi5) and Neurospor ...
DOI:
10.1007/BF00313431
PubMed:
7788720

848. Phylogenetic position of the Chromista plastids based on small subunit rRNA coding regions

Author:
Medlin, L.K.; Cooper, A.; Hill, C.; Wrieden, S.; Wellbrock, U.
Source:
Current genetics 1995 v.28 no.6 pp. 560-565
ISSN:
0172-8083
Subject:
protein secondary structure,   etc   ; Skeletonema costatum; ribosomal RNA; algae; ribosomal DNA; chemotaxonomy; phylogeny; genes; nucleotide sequences; molecular conformation; chloroplasts;     Show all 11 Subjects
Abstract:
... The kingdom Chromista contains eukaryotic organisms with tubular mastigonemes on the leading flagellum of their bi-flagellated stages, and plastics within a chloroplast endoplasmic reticulum (CER). The complex series of events leading to the formation of the CER is hypothesized to have occurred only once. Thus, all organisms with plastid-CER connections are believed to be monophyletic and derived ...
DOI:
10.1007/BF00518169
PubMed:
8593687

849. The trans-spliced intron 1 in the psaA gene of the Chlamydomonas chloroplast: a comparative analysis

Author:
Turmel, M.; Choquet, Y.; Goldschmidt-Clermont, M.; Rochaix, J.D.; Otis, C.; Lemieux, C.
Source:
Current genetics 1995 v.27 no.3 pp. 270-279
ISSN:
0172-8083
Subject:
protein secondary structure,   etc   ; alternative splicing; structural genes; chloroplast DNA; exons; genomics; Chlamydomonas reinhardtii; RNA; introns; molecular conformation; chloroplasts;     Show all 11 Subjects
Abstract:
... In the secondary structure model that has been proposed for the trans-spliced intron 1 in the Chlamydomonas reinhardtii psaA gene, a third RNA species (tscA RNA) interacts with the 5' and 3' intron parts flanking the exons to reconstitute a composite structure with several features of group-II introns. To test the validity of this model, we undertook the sequencing and modelling of equivalent intr ...
DOI:
10.1007/BF00326160
PubMed:
7736613

850. Water Sorption of Gliadin

Author:
IL, BARBARA; DAUN, HENRYK; GILBERT, SEYMOUR G.
Source:
Journal of food science 1991 v.56 no.2 pp. 510-512
ISSN:
0022-1147
Subject:
protein secondary structure,   etc   ; acetic acid; gas chromatography; gliadin; hydrogen bonding; sorption; water uptake;     Show all 7 Subjects
Abstract:
... Crude wheat gliadin from acetic acid solution showed lower water sorption by pulse and frontal Inverse Gas Chromatography methods as compared to a static method but the pulse data for a highly purified Ponca wheat gliadin from ethanol agreed with static data for crude gliadin. Use of ethanol for dissolving gliadins for IGC column preparation gave sorption equivalent to the static method whereas ac ...
DOI:
10.1111/j.1365-2621.1991.tb05315.x

851. Arabidopsis thaliana contains a large family of germin-like proteins: characterization of cDNA and genomic sequences encoding 12 unique family members

Author:
Carter, Clay; Graham, Richard A.; Thornburg, Robert W.
Source:
Plant molecular biology 1998 v.38 no.6 pp. 929-943
ISSN:
0167-4412
Subject:
protein secondary structure,   etc   ; Arabidopsis thaliana; chromosomes; complementary DNA; expressed sequence tags; messenger RNA; multigene family; plant proteins; promoter regions; signal peptide; transcription (genetics); wheat;     Show all 12 Subjects
Abstract:
... We have identified 39 Arabidopsis thaliana ESTs encoding germin-like proteins (GLPs) and have completely sequenced 25 of these cDNAs. Our analysis demonstrates that the Arabidopsis genome contains a gene family with at least 12 GLP genes. Comparisons with other known germins and germin-like proteins indicate that these Arabidopsis GLP subfamilies are unique from wheat germin. All other known GLPs ...
DOI:
10.1023/A:1006038117130

852. A transcriptional activating region with two contrasting modes of protein interaction

Author:
Ansari, A.Z.; Reece, R.J.; Ptashne, M.
Source:
Proceedings of the National Academy of Sciences of the United States of America 1998 v.95 no.23 pp. 13543-13548
ISSN:
0027-8424
Subject:
protein secondary structure,   etc   ; Saccharomyces cerevisiae; transcription factors; DNA-binding proteins; cysteine; proline; mutants; molecular conformation; gene expression; reporter genes; beta-galactosidase; transcription (genetics); binding sites; site-directed mutagenesis;     Show all 14 Subjects
Abstract:
... A C-terminal segment of the yeast activator Gal4 manifests two functions: When tethered to DNA, it elicits gene activation, and it binds the inhibitor Gal80. Here we examine the effects on these two functions of cysteine and proline substitutions. We find that, although certain cysteine substitutions diminish interaction with Gal80, those substitutions have little effect on the activating function ...
DOI:
10.1073/pnas.95.23.13543
PubMed:
9811836
PubMed Central:
PMC24855

853. The cox2 locus of the primitive angiosperm plant Acorus calamus: molecular structure, transcript processing and RNA editing

Author:
Albertazzi, F.J.; Kudla, J.; Bock, R.
Source:
MGG 1998 v.259 no.6 pp. 591-600
ISSN:
0026-8925
Subject:
protein secondary structure,   etc   ; messenger RNA; alternative splicing; loci; mitochondrial DNA; phylogeny; amino acid sequences; gene expression; cytochrome-c oxidase; RNA editing; Acorus calamus; molecular conformation; introns;     Show all 13 Subjects
DOI:
10.1007/s004380050852
PubMed:
9819051

854. SIRE-1, a copia/Ty1-like retroelement from soybean, encodes a retroviral envelope-like protein

Author:
Laten, H.M.; Majumdar, A.; Gaucher, E.A.
Source:
Proceedings of the National Academy of Sciences of the United States of America 1998 v.95 no.12 pp. 6897-6902
ISSN:
0027-8424
Subject:
protein secondary structure,   etc   ; RNA-directed DNA polymerase; retrotransposons; Glycine max; Retroviridae; transmembrane proteins; open reading frames; amino acid sequences; molecular conformation;     Show all 9 Subjects
Abstract:
... The soybean genome hosts a family of several hundred, relatively homogeneous copies of a large, copia/Ty1-like retroelement designated SIRE-1. A copy of this element has been recovered from a Glycine max genomic library. DNA sequence analysis of two SIRE-1 subclones revealed that SIRE-1 contains a long, uninterrupted, ORF between the 3' end of the pol ORF and the 3' long terminal repeat (LTR), a r ...
DOI:
10.1073/pnas.95.12.6897
PubMed:
9618510
PubMed Central:
PMC22677

855. Interaction of mitochondrial RNA editing and nucleolytic processing in the restoration of male fertility in sorghum

Author:
Pring, D.R.; Chen, W.; Tang, H.V.; Howad, W.; Kempken, F.
Source:
Current genetics 1998 v.33 no.6 pp. 429-436
ISSN:
0172-8083
Subject:
protein secondary structure,   etc   ; Sorghum bicolor; messenger RNA; RNA editing; nucleases; cytoplasmic male sterility; male fertility; line differences; complementary DNA; molecular conformation; mitochondrial DNA; genomics;     Show all 12 Subjects
DOI:
10.1007/s002940050356
PubMed:
9644206

856. Processing of plant mitochondrial tRNA(Gly) and tRNA(Ser) (GCU) is independent of RNA editing

Author:
Schock, I.; Marechal-Drouard, L.; Marchfelder, A.; Binder, S.
Source:
MGG 1998 v.257 no.5 pp. 554-5560
ISSN:
0026-8925
Subject:
protein secondary structure,   etc   ; Pisum sativum; Solanum tuberosum; mitochondrial DNA; genes; transfer RNA; serine; nucleotide sequences; molecular conformation; RNA editing; chemical reactions; glycine (amino acid);     Show all 12 Subjects
DOI:
10.1007/s004380050681
PubMed:
9563841

857. Phylogeny of hard- and soft-tick taxa (Acari: Ixodida) based on mitochondrial 16S rDNA sequences

Author:
Black, W.C. IV; Piesman, J.
Source:
Proceedings of the National Academy of Sciences of the United States of America 1994 v.91 no.21 pp. 10034-10038
ISSN:
0027-8424
Subject:
protein secondary structure,   etc   ; Ixodidae; Argasidae; ribosomal DNA; ribosomal RNA; structural genes; nucleotide sequences; mitochondrial DNA; phylogeny; molecular conformation;     Show all 10 Subjects
Abstract:
... Ticks are parasitiform mites that are obligate hematophagous ectoparasites of amphibians, reptiles, birds, and mammals. A phylogeny for tick families, subfamilies, and genera has been described based on morphological characters, life histories, and host associations. To test the existing phylogeny, we sequenced approximately 460 bp from the 3' end of the mitochondrial 16S rRNA gene (rDNA) in 36 ha ...
DOI:
10.1073/pnas.91.21.10034
PubMed:
7937832
PubMed Central:
PMC44952

858. Two-dimensional 1H-NMR studies of maize lipid-transfer protein. Sequence-specific assignment and secondary structure

Author:
Petit, M.C.; Sodano, P.; Marion, D.; Ptak, M.
Source:
European journal of biochemistry 1994 v.222 no.3 pp. 1047-1054
ISSN:
0014-2956
Subject:
protein secondary structure,   etc   ; Zea mays; seeds; lipids; binding proteins; amino acid sequences; binding sites; structure-activity relationships; spectral analysis;     Show all 9 Subjects
Abstract:
... Correlation spectroscopy (COSY), total correlation spectroscopy (TOCSY) and NOE spectroscopy (NOESY) experiments have been used to assign sequentially the 1H 500-MHz NMR spectra of a non-specific (ns) lipid-transfer protein extracted from maize seeds. The spin-system identification and sequential assignment were combined with secondary-structure determination to identify most of the proton resonan ...
DOI:
10.1111/j.1432-1033.1994.tb18957.x
PubMed:
8026483

859. Equine infectious anemia virus Tat is a predominantly helica protein

Author:
Sticht, H.; Willbold, D.; Bayer, P.; Ejchart, A.; Rosin-Arbesfeld, R.; Gazit, A.; Yaniv, A.; Frank, R.; Rosch, P.
Source:
European journal of biochemistry 1993 v.218 no.3 pp. 973-976
ISSN:
0014-2956
Subject:
protein secondary structure,   etc   ; Equine infectious anemia virus; amino acid sequences; viral proteins; structure-activity relationships; spectral analysis;     Show all 6 Subjects
Abstract:
... Nuclear magnetic resonance (NMR) spectroscopy revealed features of the secondary structure of the equine infectious anemia virus (EIAV) Tat protein in solution. We could show that this protein, which is required in the replication cycle of lentiviruses, forms a predominantly helical structure in trifluoroethanol/water (40% by vol.) solution. In particular, the basic RNA-binding region and the adja ...
DOI:
10.1111/j.1432-1033.1993.tb18455.x

860. Diagonalization in a mixed basis: a method to compute low-frequency normal modes for large macromolecules

Author:
Mouawad, L.; Perahia, D.
Source:
Biopolymers 1993 v.33 no.4 pp. 599-611
ISSN:
0006-3525
Subject:
protein secondary structure,   etc   ; lysozyme; pancreas; trypsin inhibitors; cattle; alanine; neurotoxins; peptides; bacteriophages; algorithms; computer analysis; molecular conformation; Scorpiones;     Show all 13 Subjects
Abstract:
... Low-frequency collective motions in proteins are generally very important for their biological functions. To study such motions, harmonic dynamics proved most useful since it is a straightforward method; it consists of the diagonalization of the Hessian matrix of the potential energy, yielding the vibrational spectrum and the directions of internal motions. Unfortunately, the diagonalization of th ...
DOI:
10.1002/bip.360330409