Molecular and Genetic Characterization of Rf2, A
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A Chloroplast Gene Is Converted Into a Nucleargene
Proc. Nati. Acad. Sci. USA Vol. 85, pp. 391-395, January 1988 Biochemistry Relocating a gene for herbicide tolerance: A chloroplast gene is converted into a nuclear gene (QB protein/atrazine tolerance/transit peptide) ALICE Y. CHEUNG*, LAWRENCE BOGORAD*, MARC VAN MONTAGUt, AND JEFF SCHELLt: *Department of Cellular and Developmental Biology, 16 Divinity Avenue, The Biological Laboratories, Harvard University, Cambridge, MA 02138; tLaboratorium voor Genetica, Rijksuniversiteit Ghent, B-9000 Ghent, Belgium; and TMax-Planck-Institut fur Zuchtungsforschung, D-500 Cologne 30, Federal Republic of Germany Contributed by Lawrence Bogorad, September 30, 1987 ABSTRACT The chloroplast gene psbA codes for the the gene for ribulose bisphosphate carboxylase/oxygenase photosynthetic quinone-binding membrane protein Q which can transport the protein product into chloroplasts (5). We is the target of the herbicide atrazine. This gene has been have spliced the coding region of the psbA gene isolated converted into a nuclear gene. The psbA gene from an from the chloroplast DNA of the atrazine-resistant biotype atrazine-resistant biotype of Amaranthus hybridus has been of Amaranthus to the transcriptional-control and transit- modified by fusing its coding region to transcription- peptide-encoding regions of a nuclear gene, ss3.6, for the regulation and transit-peptide-encoding sequences of a bona SSU of ribulose bisphosphate carboxylase/oxygenase of pea fide nuclear gene. The constructs were introduced into the (6). The fusion-gene constructions (designated SSU-ATR) nuclear genome of tobacco by using the Agrobacteium tumor- were introduced into tobacco plants via the Agrobacterium inducing (Ti) plasmid system, and the protein product of tumor-inducing (Ti) plasmid transformation system using the nuclear psbA has been identified in the photosynthetic mem- disarmed Ti plasmid vector pGV3850 (7). -
The Molecular Basis of Cytoplasmic Male Sterility and Fertility Restoration Patrick S
trends in plant science reviews 24 Grandmougin, A. et al. (1989) Cyclopropyl sterols and phospholipid 34 Gachotte, D., Meens, R. and Benveniste, P. (1995) An Arabodopsis mutant composition of membrane fractions from maize roots treated with deficient in sterol biosynthesis: heterologous complementation by ERG3 fenpropimorph, Plant Physiol. 90, 591–597 encoding a ⌬7-sterol-C5-desaturase from yeast, Plant J. 8, 407–416 25 Schuler, I. et al. (1990) Soybean phosphatidylcholine vesicles containing 35 Schaller, H. et al. (1995) Expression of the Hevea brasiliensis (H.B.K.) Müll. plant sterols: a fluorescence anisotropy study, Biochim. Biophys. Acta 1028, Arg. 3-hydroxy-3-methylglutaryl coenzyme A reductase 1 in tobacco results in 82–88 sterol overproduction, Plant Physiol. 109, 761–770 26 Schuler, I. et al. (1991) Differential effects of plant sterols on water 36 Marsan, M.P., Muller, I. and Milon, A. (1996) Ability of clionasterol and permeability and on acyl chain ordering of soybean phosphatidylcholine poriferasterol (24-epimers of sitosterol and stigmasterol) to regulate membrane bilayers, Proc. Natl. Acad. Sci. U. S. A. 88, 6926–6930 lipid dynamics, Chem. Phys. Lipids 84, 117–121 27 Krajewsky-Bertrand, M-A., Milon, A. and Hartmann, M-A. (1992) 37 Goad, L.J. (1990) Application of sterol synthesis inhibitors to investigate the Deuterium-NMR investigation of plant sterol effects on soybean sterol requirements of protozoa and plants, Biochem. Soc. Trans. 18, 63–65 phosphatidylcholine acyl chain ordering, Chem. Phys. Lipids 63, 235–241 38 Cerana, R. et al. (1984) Regulating effects of brassinosteroids and of sterols 28 Grandmougin-Ferjani, A., Schuler-Muller, I. -
Family Proteins Are Required for RNA Editing in Mitochondria and Plastids of Plants
Correction PLANT BIOLOGY Correction for “Multiple organellar RNA editing factor issue 13, March 27, 2012, of Proc Natl Acad Sci USA (109: (MORF) family proteins are required for RNA editing in 5104–5109; first published March 12, 2012; 10.1073/pnas. mitochondria and plastids of plants,” by Mizuki Takenaka, 1202452109). Anja Zehrmann, Daniil Verbitskiy, Matthias Kugelmann, The authors note that Fig. 2 appeared incorrectly. The cor- Barbara Härtel, and Axel Brennicke, which appeared in rected Fig. 2 and its legend appear below. Fig. 2. The MORF family of proteins contains nine genes and a potential pseudogene in A. thaliana.(A) The cladogram of similarities between the MORF proteins shows that the plastid editing factors MORF2 and MORF9 are rather distant from each other and more similar to the mitochondrial proteins MORF3 and MORF1, respectively. Predictions (marked mt or cp) and experi- mental data obtained by GFP-fusion protein localization (only MORF2) or proteomics MS data (marked with an asterisk) for the respective organellar locations are indicated. The MORF8 protein encoded by At3g15000 has been found in mitochondria in three independent assays. Proteins investigated here for their function are boxed. The conserved ∼100-amino acids domain is shaded; the other sequences show much less conservation (SI Appendix, Fig. S2). The potential pseudogene (At1g53260) contains only the C-terminal part of this conserved region. (B) Exon structures of the MORF3, MORF4 and MORF6 genes are similar to the MORF1 locus and contribute similar frag- ments but differ in their C-terminal extensions. MORF3 is a mitochondrial editing factor involved at more than 40 sites. -
BASIC GENETICS for the CLINICAL NEUROLOGIST M R Placzek, T T Warner *Ii5
J Neurol Neurosurg Psychiatry: first published as 10.1136/jnnp.73.suppl_2.ii5 on 1 December 2002. Downloaded from BASIC GENETICS FOR THE CLINICAL NEUROLOGIST M R Placzek, T T Warner *ii5 J Neurol Neurosurg Psychiatry 2002;73(Suppl II):ii5–ii11 o the casual observer, the clinical neurologist and molecular geneticist would appear very dif- ferent species. On closer inspection, however, they actually have a number of similarities: they Tboth use a rather impenetrable language littered with abbreviations, publish profusely with- out seeming to alter the course of clinical medicine, and make up a small clique regarded as rather esoteric by their peers. In reality, they are both relatively simple creatures who rely on basic sets of rules to work in their specialities. Indeed they have had a productive symbiotic relationship in recent years and the application of molecular biological techniques to clinical neuroscience has had a profound impact on the understanding of the pathophysiology of many neurological diseases. One reason for this is that around one third of recognisable mendelian disease traits demonstrate phenotypic expression in the nervous system. The purpose of this article is to demystify the basic rules of molecular biology, and allow the clinical neurologist to gain a better understanding of the techniques which have led to the isola- tion (cloning) of neurological disease genes and the potential uses of this knowledge. c NUCLEIC ACIDS Deoxyribonucleic acid (DNA) is the macromolecule that stores the blueprint for all the proteins of the body. It is responsible for development and physical appearance, and controls every biological copyright. -
“Subfossil” Koala Lemur Megaladapis Edwardsi
Evolutionary and phylogenetic insights from a nuclear genome sequence of the extinct, giant, “subfossil” koala lemur Megaladapis edwardsi Stephanie Marciniaka, Mehreen R. Mughalb, Laurie R. Godfreyc, Richard J. Bankoffa, Heritiana Randrianatoandroa,d, Brooke E. Crowleye,f, Christina M. Bergeya,g,h, Kathleen M. Muldooni, Jeannot Randrianasyd, Brigitte M. Raharivololonad, Stephan C. Schusterj, Ripan S. Malhik,l, Anne D. Yoderm,n, Edward E. Louis Jro,1, Logan Kistlerp,1, and George H. Perrya,b,g,q,1 aDepartment of Anthropology, Pennsylvania State University, University Park, PA 16802; bBioinformatics and Genomics Intercollege Graduate Program, Pennsylvania State University, University Park, PA 16082; cDepartment of Anthropology, University of Massachusetts, Amherst, MA 01003; dMention Anthropobiologie et Développement Durable, Faculté des Sciences, Université d’Antananarivo, Antananarivo 101, Madagascar; eDepartment of Geology, University of Cincinnati, Cincinnati, OH 45220; fDepartment of Anthropology, University of Cincinnati, Cincinnati, OH 45220; gDepartment of Biology, Pennsylvania State University, University Park, PA 16802; hDepartment of Genetics, Rutgers University, New Brunswick, NJ 08854; iDepartment of Anatomy, Midwestern University, Glendale, AZ 85308; jSingapore Centre for Environmental Life Sciences Engineering, Nanyang Technological University, Singapore 639798; kDepartment of Anthropology, University of Illinois Urbana–Champaign, Urbana, IL 61801; lDepartment of Ecology, Evolution and Behavior, Carl R. Woese Institute for -
SATMF Suppresses the Premature Senescence Phenotype of the ATM Loss-Of-Function Mutant and Improves Its Fertility in Arabidopsis
Supplementary Materials SATMF Suppresses the Premature Senescence Phenotype of the ATM Loss-of-Function Mutant and Improves Its Fertility in Arabidopsis Yi Zhang, Hou-Ling Wang, Yuhan Gao, Hongwei Guo and Zhonghai Li Figure S1. Histological GUS staining analysis of gene expression of ATM at different developmental stages. (A) Rosette leaves of 8-day-old seedling of pATM-GUS/Col-0. (B) Rosette leaves of 16-day-old plant of pATM-GUS/Col-0. (C) Rosette leaves of 48-day-old plant of pATM-GUS/Col-0. Int. J. Mol. Sci. 2020, 21, x; doi: FOR PEER REVIEW www.mdpi.com/journal/ijms Int. J. Mol. Sci. 2020, 21, x FOR PEER REVIEW 2 of 5 Figure S2. Screen for suppressor of atm mutant in fertility (satmf) by EMS. (A) Experimental design for screening the expected phenotypes of stamf mutants. (B) EMS mutagenesis of atm-2 seeds by using different experimental conditions. (C) Seeds of atm-2 mutant is hypersensitive to EMS in comparison to Col-0. Int. J. Mol. Sci. 2020, 21, x FOR PEER REVIEW 3 of 5 Figure S3. Molecular identification of satmf mutants. (A) Fertility of plants of Col-0, atm-2, satmf1, satmf2 and satmf3. (B) Genotyping analysis of atm-2, satmf1, satmf2 and satmf3 plants. (C) Confirmation of the backgrounds of satmf1, satmf2 and satmf3 plants by sequencing analysis of PCR products in (B). The “G” PCR reaction tests for the ability to amplify a genome region that will be present in wild type and heterozygous lines, but will not amplify in homozygous lines. -
DNA Interstrand Cross-Links Induced by Psoralen Are Not Repaired in Mammalian Mitochondria
[CANCER RESEARCH 58. 1400-1404, April 1. 1998) Advances in Brief DNA Interstrand Cross-Links Induced by Psoralen Are Not Repaired in Mammalian Mitochondria Carleen Cullinane and Vilhelm A. Bohr1 Department of Biochemistry, Lit Trohe University, Bundoora, Victoria, 3083, Australia 1C. C./; and Laboratory of Molecular Genetics, National Institutes on Aging. Baltimore. Maryland 21224 ¡C.C., V.A. B.] Abstract evidence suggests that mitochondria are capable of repairing some types of DNA lesions. DNA damage induced by A'-methyl purines, Although it is generally known that mitochondria are defective in DNA including streptozotocin and /V-methyl-yV-nitrosourea, which, in nu damage processing, little is known about the DNA repair pathways and clear DNA, are substrates for the base excision repair pathway, are mechanisms that exist in these vital organdÃes. Certain lesions that are repaired in mitochondria (3). The efficient in vivo removal of O6- removed by base excision repair are efficiently removed in mitochondria, ethyl-guanine lesions induced by ethyl nitrosourea in rat mitochondria whereas some bulky lesions that are removed by nucleotide excision repair are not repaired in these organelles. There has been much interest in has also been clearly demonstrated (4). Oxidative DNA lesions in whether mitochondria possess activities for recombination repair, and duced by alloxan (5) and bleomycin (6) are also efficiently repaired in some previous studies have reported such activities, whereas others have mitochondria. In contrast, bulky lesions induced by UVC, nitrogen not. We have taken the approach of studying the formation and removal mustard, and cisplatin are apparently not repaired by mitochondria of ¡nterstrand cross-links (ICLs) in DNA. -
Two CRM Protein Subfamilies Cooperate in the Splicing of Group IIB Introns in Chloroplasts
JOBNAME: RNA 14#11 2008 PAGE: 1 OUTPUT: Wednesday September 17 14:17:18 2008 csh/RNA/170257/rna12237 Downloaded from rnajournal.cshlp.org on September 29, 2021 - Published by Cold Spring Harbor Laboratory Press Two CRM protein subfamilies cooperate in the splicing of group IIB introns in chloroplasts YUKARI ASAKURA, OMER ALI BAYRAKTAR, and ALICE BARKAN Institute of Molecular Biology, University of Oregon, Eugene, Oregon 97403, USA ABSTRACT Chloroplast genomes in angiosperms encode ;20 group II introns, approximately half of which are classified as subgroup IIB. The splicing of all but one of the subgroup IIB introns requires a heterodimer containing the peptidyl-tRNA hydrolase homolog CRS2 and one of two closely related proteins, CAF1 or CAF2, that harbor a recently recognized RNA binding domain called the CRM domain. Two CRS2/CAF-dependent introns require, in addition, a CRM domain protein called CFM2 that is only distantly related to CAF1 and CAF2. Here, we show that CFM3, a close relative of CFM2, associates in vivo with those CRS2/CAF- dependent introns that are not CFM2 ligands. Mutant phenotypes in rice and Arabidopsis support a role for CFM3 in the splicing of most of the introns with which it associates. These results show that either CAF1 or CAF2 and either CFM2 or CFM3 simultaneously bind most chloroplast subgroup IIB introns in vivo, and that the CAF and CFM subunits play nonredundant roles in splicing. These results suggest that the expansion of the CRM protein family in plants resulted in two subfamilies that play different roles in group II intron splicing, with further diversification within a subfamily to accommodate multiple intron ligands. -
Molecular and Supramolecular Structure of the Mitochondrial Oxidative Phosphorylation System: Implications for Pathology
life Review Molecular and Supramolecular Structure of the Mitochondrial Oxidative Phosphorylation System: Implications for Pathology Salvatore Nesci 1,* , Fabiana Trombetti 1, Alessandra Pagliarani 1,*, Vittoria Ventrella 1, Cristina Algieri 1 , Gaia Tioli 2 and Giorgio Lenaz 2,* 1 Department of Veterinary Medical Sciences, Alma Mater Studiorum University of Bologna, 40064 Ozzano Emilia, Italy; [email protected] (F.T.); [email protected] (V.V.); [email protected] (C.A.) 2 Department of Biomedical and Neuromotor Sciences, Alma Mater Studiorum University of Bologna, 40138 Bologna, Italy; [email protected] * Correspondence: [email protected] (S.N.); [email protected] (A.P.); [email protected] (G.L.) Abstract: Under aerobic conditions, mitochondrial oxidative phosphorylation (OXPHOS) converts the energy released by nutrient oxidation into ATP, the currency of living organisms. The whole biochemical machinery is hosted by the inner mitochondrial membrane (mtIM) where the protonmo- tive force built by respiratory complexes, dynamically assembled as super-complexes, allows the F1FO-ATP synthase to make ATP from ADP + Pi. Recently mitochondria emerged not only as cell powerhouses, but also as signaling hubs by way of reactive oxygen species (ROS) production. How- ever, when ROS removal systems and/or OXPHOS constituents are defective, the physiological ROS generation can cause ROS imbalance and oxidative stress, which in turn damages cell components. Citation: Nesci, S.; Trombetti, F.; Moreover, the morphology of mitochondria rules cell fate and the formation of the mitochondrial Pagliarani, A.; Ventrella, V.; Algieri, permeability transition pore in the mtIM, which, most likely with the F F -ATP synthase contribu- C.; Tioli, G.; Lenaz, G. -
Human Genetics '99: Trinucleotide Repeats
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector Am. J. Hum. Genet. 64:354–359, 1999 HUMAN GENETICS ’99: TRINUCLEOTIDE REPEATS Fragile Sites—Cytogenetic Similarity with Molecular Diversity Grant R. Sutherland and Robert I. Richards Department of Cytogenetics and Molecular Genetics, Women’s and Children’s Hospital, Adelaide, Australia When examined in metaphase chromosome prepara- of their cytogenetic and molecular properties are given tions, all fragile sites appear as a gap or discontinuity in table 1. in chromosome structure. These gaps, which are induced Fragile sites are identifiable as gaps or chromosomal by several specific treatments of cultured cells, are of breaks in only a fraction of metaphase spreads from a variable width and promote chromosome breakage with given individual. At one extreme is FRA16B, which, variable efficiency. Within a single metaphase, it is not when induced by berenil, may be found in 190% of possible to distinguish between a fragile site and random metaphases (Schmid et al. 1986). At the opposite end of chromosomal damage. Only the statistically significant the spectrum are the common aphidicolin fragile sites. recurrence of a lesion at the same locus and under the Even the most conspicuous of these, FRA3B, is rarely same culture conditions delineates fragile sites. Several seen in 110% of metaphases (Smeets et al. 1986), and classes of fragile sites have now been characterized at many of the other common fragile sites are seen in !5% the molecular level. The “rare” fragile sites contain tan- of metaphases. Whatever the mechanisms are that result demly repeated sequences of varying complexity, which in fragile-site expression, they usually operate success- undergo expansions or, occasionally, contractions. -
Solitary Fibrous Tumors: Loss of Chimeric Protein Expression and Genomic Instability Mark Dedifferentiation
Modern Pathology (2015) 28, 1074–1083 1074 © 2015 USCAP, Inc All rights reserved 0893-3952/15 $32.00 Solitary fibrous tumors: loss of chimeric protein expression and genomic instability mark dedifferentiation Gian P Dagrada1, Rosalin D Spagnuolo1, Valentina Mauro1,6, Elena Tamborini2, Luca Cesana2, Alessandro Gronchi3, Silvia Stacchiotti4, Marco A Pierotti5,7, Tiziana Negri1,8 and Silvana Pilotti1,8 1Laboratory of Experimental Molecular Pathology, Department of Diagnostic Pathology and Laboratory, Fondazione IRCCS Istituto Nazionale dei Tumori, Milan, Italy; 2Department of Diagnostic Pathology and Laboratory, Fondazione IRCCS Istituto Nazionale dei Tumori, Milan, Italy; 3Department of Surgery, Fondazione IRCCS Istituto Nazionale dei Tumori, Milan, Italy; 4Adult Mesenchymal Tumor Medical Oncology Unit, Cancer Medicine Department, Fondazione IRCCS Istituto Nazionale dei Tumori, Milan, Italy and 5Scientific Directorate, Fondazione IRCCS Istituto Nazionale dei Tumori, Milan, Italy Solitary fibrous tumors, which are characterized by their broad morphological spectrum and unpredictable behavior, are rare mesenchymal neoplasias that are currently divided into three main variants that have the NAB2-STAT6 gene fusion as their unifying molecular lesion: usual, malignant and dedifferentiated solitary fibrous tumors. The aims of this study were to validate molecular and immunohistochemical/biochemical approaches to diagnose the range of solitary fibrous tumors by focusing on the dedifferentiated variant, and to reveal the genetic events associated with dedifferentiation by integrating the findings of array comparative genomic hybridization. We studied 29 usual, malignant and dedifferentiated solitary fibrous tumors from 24 patients (including paired samples from five patients whose tumors progressed to the dedifferentiated form) by means of STAT6 immunohistochemistry and (when frozen material was available) reverse-transcriptase polymerase chain reaction and biochemistry. -
Mitochondrial Permeability Transition: a Molecular Lesion with Multiple Drug Targets
Mitochondrial permeability transition: a molecular lesion with multiple drug targets Authors Thomas Briston1*, David Selwood2, Gyorgy Szabadkai3,4,5, Michael R Duchen3 1 Neurology Innovation Centre, Hatfield Research Laboratories, Eisai Ltd., Hatfield, UK 2 Wolfson Institute for Biomedical Research, Division of Medicine, University College London, London, UK 3 Department of Cell and Developmental Biology, Consortium for Mitochondrial Research, University College London, London, UK 4 Department of Biomedical Sciences, University of Padua, Padua, Italy 5 The Francis Crick Institute, London, UK * Correspondence: [email protected] (Thomas Briston) Key words: mitochondria, mPTP, cyclophilin D, drug discovery, calcium Abstract Mitochondrial permeability transition, as the consequence of opening of a mitochondrial permeability transition pore (mPTP), is a cellular catastrophe. Initiating bioenergetic collapse and cell death, it has been implicated in the pathophysiology of major human diseases, including neuromuscular diseases of childhood, ischaemia-reperfusion injury and age related neurodegenerative disease. mPTP represents a major therapeutic target, as opening can be prevented by a number of compounds. However, clinical studies have so far been disappointing. We therefore address the prospects and challenges faced in translating in vitro findings to clinical benefit. We review the role of mPTP opening in disease, discuss recent findings defining the putative structure of mPTP and explore strategies to identify 1 novel, clinically