Eukaryotic Genome Annotation
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PPR Proteins – Orchestrators of Organelle RNA Metabolism Aleix
1 PPR proteins – orchestrators of organelle RNA metabolism 2 Aleix Gorchs Rovira and Alison G Smith* 3 Department of Plant Sciences, University of Cambridge, Downing Street, Cambridge CB2 3EA UK 4 Correspondence 5 *Corresponding author, 6 e-mail: [email protected] 7 8 Pentatricopeptide repeat (PPR) proteins are important RNA regulators in chloroplasts and mitochondria, 9 aiding in RNA editing, maturation, stabilisation or intron splicing, and in transcription and translation 10 of organellar genes. In this review, we summarise all PPR proteins documented so far in plants and the 11 green alga Chlamydomonas. By further analysis of the known target RNAs from Arabidopsis thaliana 12 PPR proteins, we find that all organellar-encoded complexes are regulated by these proteins, although 13 to differing extents. In particular, the orthologous complexes of NADH dehydrogenase (Complex I) in 14 the mitochondria and NADH dehydrogenase-like (NDH) complex in the chloroplast were the most 15 regulated, with respectively 60 and 28% of all characterised A. thaliana PPR proteins targeting their 16 genes. 17 Abbreviations – CMS, Cytoplasm Male Sterility; PMT, Post-transcriptional modification; T/P/OPR, 18 tetra-, penta-, octo-tricopeptide repeat. 19 20 The need to regulate organelle genetic expression 21 Photosynthesis and respiration, which arose initially in prokaryotic organisms, requires the assembly of 22 many different components to form functional protein complexes (Vermaas 2001) and networks for 23 effective electron transfer (Anraku 1988). After the endosymbiotic events in which a free-living 24 cyanobacterium and an alpha-proteobacterium gave rise respectively to the chloroplasts and 25 mitochondria found in eukaryotic cells, there was migration of essential genes from the “new organelle” 26 to the nucleus. -
TAL Effectors Are Remote Controls for Gene Activation Heidi Scholze and Jens Boch
Available online at www.sciencedirect.com TAL effectors are remote controls for gene activation Heidi Scholze and Jens Boch TAL (transcription activator-like) effectors constitute a novel typically 34 amino acids (aa) long, but also repeat types of class of DNA-binding proteins with predictable specificity. They 30–42 aa can be found ([2], Figure 2). The last repeat is are employed by Gram-negative plant-pathogenic bacteria of only a half repeat. Repeat-to-repeat variations are limited the genus Xanthomonas which translocate a cocktail of to a few aa positions including two hypervariable residues different effector proteins via a type III secretion system (T3SS) at positions 12 and 13 per repeat. Typically, TALs differ into plant cells where they serve as virulence determinants. in their number of repeats while most contain 15.5–19.5 Inside the plant cell, TALs localize to the nucleus, bind to target repeats [2]. The repeat domain determines the specificity promoters, and induce expression of plant genes. DNA-binding of TALs which is mediated by selective DNA binding specificity of TALs is determined by a central domain of tandem [7,8]. TAL repeats constitute a novel type of DNA- repeats. Each repeat confers recognition of one base pair (bp) binding domain [7] distinct from classical zinc finger, in the DNA. Rearrangement of repeat modules allows design of helix–turn–helix, and leucine zipper motifs. proteins with desired DNA-binding specificities. Here, we summarize how TAL specificity is encoded, first structural data The recent understanding of the DNA-recognition speci- and first data on site-specific TAL nucleases. -
Modern Trends in Plant Genome Editing: an Inclusive Review of the CRISPR/Cas9 Toolbox
International Journal of Molecular Sciences Review Modern Trends in Plant Genome Editing: An Inclusive Review of the CRISPR/Cas9 Toolbox Ali Razzaq 1 , Fozia Saleem 1, Mehak Kanwal 2, Ghulam Mustafa 1, Sumaira Yousaf 2, Hafiz Muhammad Imran Arshad 2, Muhammad Khalid Hameed 3, Muhammad Sarwar Khan 1 and Faiz Ahmad Joyia 1,* 1 Centre of Agricultural Biochemistry and Biotechnology (CABB), University of Agriculture, Faisalabad 38040, Pakistan 2 Nuclear Institute for Agriculture and Biology (NIAB), P.O. Box 128, Faisalabad 38000, Pakistan 3 School of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai 200240, China * Correspondence: [email protected] Received: 14 June 2019; Accepted: 15 August 2019; Published: 19 August 2019 Abstract: Increasing agricultural productivity via modern breeding strategies is of prime interest to attain global food security. An array of biotic and abiotic stressors affect productivity as well as the quality of crop plants, and it is a primary need to develop crops with improved adaptability, high productivity, and resilience against these biotic/abiotic stressors. Conventional approaches to genetic engineering involve tedious procedures. State-of-the-art OMICS approaches reinforced with next-generation sequencing and the latest developments in genome editing tools have paved the way for targeted mutagenesis, opening new horizons for precise genome engineering. Various genome editing tools such as transcription activator-like effector nucleases (TALENs), zinc-finger nucleases (ZFNs), and meganucleases (MNs) have enabled plant scientists to manipulate desired genes in crop plants. However, these approaches are expensive and laborious involving complex procedures for successful editing. Conversely, CRISPR/Cas9 is an entrancing, easy-to-design, cost-effective, and versatile tool for precise and efficient plant genome editing. -
Appendix 2. Significantly Differentially Regulated Genes in Term Compared with Second Trimester Amniotic Fluid Supernatant
Appendix 2. Significantly Differentially Regulated Genes in Term Compared With Second Trimester Amniotic Fluid Supernatant Fold Change in term vs second trimester Amniotic Affymetrix Duplicate Fluid Probe ID probes Symbol Entrez Gene Name 1019.9 217059_at D MUC7 mucin 7, secreted 424.5 211735_x_at D SFTPC surfactant protein C 416.2 206835_at STATH statherin 363.4 214387_x_at D SFTPC surfactant protein C 295.5 205982_x_at D SFTPC surfactant protein C 288.7 1553454_at RPTN repetin solute carrier family 34 (sodium 251.3 204124_at SLC34A2 phosphate), member 2 238.9 206786_at HTN3 histatin 3 161.5 220191_at GKN1 gastrokine 1 152.7 223678_s_at D SFTPA2 surfactant protein A2 130.9 207430_s_at D MSMB microseminoprotein, beta- 99.0 214199_at SFTPD surfactant protein D major histocompatibility complex, class II, 96.5 210982_s_at D HLA-DRA DR alpha 96.5 221133_s_at D CLDN18 claudin 18 94.4 238222_at GKN2 gastrokine 2 93.7 1557961_s_at D LOC100127983 uncharacterized LOC100127983 93.1 229584_at LRRK2 leucine-rich repeat kinase 2 HOXD cluster antisense RNA 1 (non- 88.6 242042_s_at D HOXD-AS1 protein coding) 86.0 205569_at LAMP3 lysosomal-associated membrane protein 3 85.4 232698_at BPIFB2 BPI fold containing family B, member 2 84.4 205979_at SCGB2A1 secretoglobin, family 2A, member 1 84.3 230469_at RTKN2 rhotekin 2 82.2 204130_at HSD11B2 hydroxysteroid (11-beta) dehydrogenase 2 81.9 222242_s_at KLK5 kallikrein-related peptidase 5 77.0 237281_at AKAP14 A kinase (PRKA) anchor protein 14 76.7 1553602_at MUCL1 mucin-like 1 76.3 216359_at D MUC7 mucin 7, -
STACK: a Toolkit for Analysing Β-Helix Proteins
STACK: a toolkit for analysing ¯-helix proteins Master of Science Thesis (20 points) Salvatore Cappadona, Lars Diestelhorst Abstract ¯-helix proteins contain a solenoid fold consisting of repeated coils forming parallel ¯-sheets. Our goal is to formalise the intuitive notion of a ¯-helix in an objective algorithm. Our approach is based on first identifying residues stacks — linear spatial arrangements of residues with similar conformations — and then combining these elementary patterns to form ¯-coils and ¯-helices. Our algorithm has been implemented within STACK, a toolkit for analyzing ¯-helix proteins. STACK distinguishes aromatic, aliphatic and amidic stacks such as the asparagine ladder. Geometrical features are computed and stored in a relational database. These features include the axis of the ¯-helix, the stacks, the cross-sectional shape, the area of the coils and related packing information. An interface between STACK and a molecular visualisation program enables structural features to be highlighted automatically. i Contents 1 Introduction 1 2 Biological Background 2 2.1 Basic Concepts of Protein Structure ....................... 2 2.2 Secondary Structure ................................ 2 2.3 The ¯-Helix Fold .................................. 3 3 Parallel ¯-Helices 6 3.1 Introduction ..................................... 6 3.2 Nomenclature .................................... 6 3.2.1 Parallel ¯-Helix and its ¯-Sheets ..................... 6 3.2.2 Stacks ................................... 8 3.2.3 Coils ..................................... 8 3.2.4 The Core Region .............................. 8 3.3 Description of Known Structures ......................... 8 3.3.1 Helix Handedness .............................. 8 3.3.2 Right-Handed Parallel ¯-Helices ..................... 13 3.3.3 Left-Handed Parallel ¯-Helices ...................... 19 3.4 Amyloidosis .................................... 20 4 The STACK Toolkit 24 4.1 Identification of Structural Elements ....................... 24 4.1.1 Stacks ................................... -
An Overview of Pentatricopeptide Repeat Proteins and Their Applications
Biochimie 113 (2015) 93e99 Contents lists available at ScienceDirect Biochimie journal homepage: www.elsevier.com/locate/biochi Review An overview of pentatricopeptide repeat proteins and their applications Sam Manna Department of Microbiology, La Trobe University, Melbourne, Victoria, Australia article info abstract Article history: Pentatricopeptide repeat (PPR) proteins are a large family of modular RNA-binding proteins which Received 19 February 2015 mediate several aspects of gene expression primarily in organelles but also in the nucleus. These proteins Accepted 3 April 2015 facilitate processing, splicing, editing, stability and translation of RNAs. While major advances in PPR Available online 14 April 2015 research have been achieved with plant PPR proteins, the significance of non-plant PPR proteins is becoming of increasing importance. PPR proteins are classified into different subclasses based on their Keywords: domain architecture, which is often a reflection of their function. This review provides an overview of the Pentatricopeptide repeat protein significant findings regarding the functions, evolution and applications of PPR proteins. Horizontal gene Mitochondria Chloroplast transfer appears to have played a major role in the sporadic phylogenetic distribution of different PPR Horizontal gene transfer subclasses in both eukaryotes and prokaryotes. Additionally, the use of synthetic biology and protein tRNA guanine methyltransferase engineering to create designer PPR proteins to control gene expression in vivo is discussed. This review also highlights some of the aspects of PPR research that require more attention particularly in non-plant organisms. This includes the lack of research into the recently discovered PPR-TGM subclass, which is not only the first PPR subclass absent from plants but present in economically and clinically-relevant pathogens. -
Pentatricopeptide Repeat Protein MID1 Modulates Nad2 Intron 1
www.nature.com/scientificreports OPEN Pentatricopeptide repeat protein MID1 modulates nad2 intron 1 splicing and Arabidopsis development Peng Zhao1,2,3, Fang Wang1,2,3, Na Li1,2, Dong-Qiao Shi1,2 & Wei-Cai Yang 1,2* As one of the best-studied RNA binding proteins in plant, pentatricopeptide repeats (PPRs) protein are mainly targeted to mitochondria and/or chloroplasts for RNA processing to regulate the biogenesis and function of the organelles, but its molecular mechanism and role in development remain to be further revealed. Here, we identifed a mitochondria-localized P-type small PPR protein, MITOCHONDRION- MEDIATED GROWTH DEFECT 1 (MID1) that is crucial for Arabidopsis development. Mutation in MID1 causes retarded embryo development and stunted plant growth with defects in cell expansion and proliferation. Molecular experiments showed that MID1 is required for the splicing of the nad2 intron 1 in mitochondria. Consistently, mid1 plants display signifcant reduction in the abundance and activity of mitochondrial respiration complex I, accompanied by abnormal mitochondrial morphology and energy metabolism. Furthermore, MID1 is associated with other trans-factors involved in NICOTINAMIDE ADENINE DINUCLEOTIDE HYDROGEN (NADH) DEHYDROGENASE SUBUNIT 2 (nad2) intron 1 splicing, and interacts directly with itself and MITOCHONDRIAL STABILITY FACTOR 1 (MTSF1). This suggests that MID1 most likely functions as a dimer for nad2 intron 1 splicing. Together, we characterized a novel PPR protein MID1 for nad2 intron 1 splicing. Mitochondrion, originated from the gram-negative bacterium ancestors, is an essential organelle of eukaryotic organisms that can produce energy and signaling molecules for their growth and development1–3. Most of the mitochondrial genes have been transferred and integrated into nuclear genome during evolutionary progress, and the remaining genes encode a limited number of proteins that mainly make up the respiration complexes and translation machinery4–7. -
Calculating the Structure-Based Phylogenetic Relationship
CALCULATING THE STRUCTURE-BASED PHYLOGENETIC RELATIONSHIP OF DISTANTLY RELATED HOMOLOGOUS PROTEINS UTILIZING MAXIMUM LIKELIHOOD STRUCTURAL ALIGNMENT COMBINATORICS AND A NOVEL STRUCTURAL MOLECULAR CLOCK HYPOTHESIS A DISSERTATION IN Molecular Biology and Biochemistry and Cell Biology and Biophysics Presented to the Faculty of the University of Missouri-Kansas City in partial fulfillment of the requirements for the degree Doctor of Philosophy by SCOTT GARRETT FOY B.S., Southwest Baptist University, 2005 B.A., Truman State University, 2007 M.S., University of Missouri-Kansas City, 2009 Kansas City, Missouri 2013 © 2013 SCOTT GARRETT FOY ALL RIGHTS RESERVED CALCULATING THE STRUCTURE-BASED PHYLOGENETIC RELATIONSHIP OF DISTANTLY RELATED HOMOLOGOUS PROTEINS UTILIZING MAXIMUM LIKELIHOOD STRUCTURAL ALIGNMENT COMBINATORICS AND A NOVEL STRUCTURAL MOLECULAR CLOCK HYPOTHESIS Scott Garrett Foy, Candidate for the Doctor of Philosophy Degree University of Missouri-Kansas City, 2013 ABSTRACT Dendrograms establish the evolutionary relationships and homology of species, proteins, or genes. Homology modeling, ligand binding, and pharmaceutical testing all depend upon the homology ascertained by dendrograms. Regardless of the specific algorithm, all dendrograms that ascertain protein evolutionary homology are generated utilizing polypeptide sequences. However, because protein structures superiorly conserve homology and contain more biochemical information than their associated protein sequences, I hypothesize that utilizing the structure of a protein instead -
And Beta-Helical Protein Motifs
Soft Matter Mechanical Unfolding of Alpha- and Beta-helical Protein Motifs Journal: Soft Matter Manuscript ID SM-ART-10-2018-002046.R1 Article Type: Paper Date Submitted by the 28-Nov-2018 Author: Complete List of Authors: DeBenedictis, Elizabeth; Northwestern University Keten, Sinan; Northwestern University, Mechanical Engineering Page 1 of 10 Please doSoft not Matter adjust margins Soft Matter ARTICLE Mechanical Unfolding of Alpha- and Beta-helical Protein Motifs E. P. DeBenedictis and S. Keten* Received 24th September 2018, Alpha helices and beta sheets are the two most common secondary structure motifs in proteins. Beta-helical structures Accepted 00th January 20xx merge features of the two motifs, containing two or three beta-sheet faces connected by loops or turns in a single protein. Beta-helical structures form the basis of proteins with diverse mechanical functions such as bacterial adhesins, phage cell- DOI: 10.1039/x0xx00000x puncture devices, antifreeze proteins, and extracellular matrices. Alpha helices are commonly found in cellular and extracellular matrix components, whereas beta-helices such as curli fibrils are more common as bacterial and biofilm matrix www.rsc.org/ components. It is currently not known whether it may be advantageous to use one helical motif over the other for different structural and mechanical functions. To better understand the mechanical implications of using different helix motifs in networks, here we use Steered Molecular Dynamics (SMD) simulations to mechanically unfold multiple alpha- and beta- helical proteins at constant velocity at the single molecule scale. We focus on the energy dissipated during unfolding as a means of comparison between proteins and work normalized by protein characteristics (initial and final length, # H-bonds, # residues, etc.). -
Introduction to the Local Theory of Curves and Surfaces
Introduction to the Local Theory of Curves and Surfaces Notes of a course for the ICTP-CUI Master of Science in Mathematics Marco Abate, Fabrizio Bianchi (with thanks to Francesca Tovena) (Much more on this subject can be found in [1]) CHAPTER 1 Local theory of curves Elementary geometry gives a fairly accurate and well-established notion of what is a straight line, whereas is somewhat vague about curves in general. Intuitively, the difference between a straight line and a curve is that the former is, well, straight while the latter is curved. But is it possible to measure how curved a curve is, that is, how far it is from being straight? And what, exactly, is a curve? The main goal of this chapter is to answer these questions. After comparing in the first two sections advantages and disadvantages of several ways of giving a formal definition of a curve, in the third section we shall show how Differential Calculus enables us to accurately measure the curvature of a curve. For curves in space, we shall also measure the torsion of a curve, that is, how far a curve is from being contained in a plane, and we shall show how curvature and torsion completely describe a curve in space. 1.1. How to define a curve n What is a curve (in a plane, in space, in R )? Since we are in a mathematical course, rather than in a course about military history of Prussian light cavalry, the only acceptable answer to such a question is a precise definition, identifying exactly the objects that deserve being called curves and those that do not. -
An Unusual Hydrophobic Core Confers Extreme Flexibility to HEAT Repeat Proteins
1596 Biophysical Journal Volume 99 September 2010 1596–1603 An Unusual Hydrophobic Core Confers Extreme Flexibility to HEAT Repeat Proteins Christian Kappel, Ulrich Zachariae, Nicole Do¨lker, and Helmut Grubmu¨ller* Department of Theoretical and Computational Biophysics, Max Planck Institute for Biophysical Chemistry, Go¨ttingen, Germany ABSTRACT Alpha-solenoid proteins are suggested to constitute highly flexible macromolecules, whose structural variability and large surface area is instrumental in many important protein-protein binding processes. By equilibrium and nonequilibrium molecular dynamics simulations, we show that importin-b, an archetypical a-solenoid, displays unprecedentedly large and fully reversible elasticity. Our stretching molecular dynamics simulations reveal full elasticity over up to twofold end-to-end extensions compared to its bound state. Despite the absence of any long-range intramolecular contacts, the protein can return to its equilibrium structure to within 3 A˚ backbone RMSD after the release of mechanical stress. We find that this extreme degree of flexibility is based on an unusually flexible hydrophobic core that differs substantially from that of structurally similar but more rigid globular proteins. In that respect, the core of importin-b resembles molten globules. The elastic behavior is dominated by nonpolar interactions between HEAT repeats, combined with conformational entropic effects. Our results suggest that a-sole- noid structures such as importin-b may bridge the molecular gap between completely structured and intrinsically disordered proteins. INTRODUCTION Solenoid proteins, consisting of repeating arrays of simple on repeat proteins focus on the folding and unfolding basic structural motifs, account for >5% of the genome of mechanism (14–16), an atomic force microscopy study on multicellular organisms (1). -
Chern-Simons-Higgs Model As a Theory of Protein Molecules
ITEP-TH-12/19 Chern-Simons-Higgs Model as a Theory of Protein Molecules Dmitry Melnikov and Alyson B. F. Neves November 13, 2019 Abstract In this paper we discuss a one-dimensional Abelian Higgs model with Chern-Simons interaction as an effective theory of one-dimensional curves embedded in three-dimensional space. We demonstrate how this effective model is compatible with the geometry of protein molecules. Using standard field theory techniques we analyze phenomenologically interesting static configurations of the model and discuss their stability. This simple model predicts some characteristic relations for the geometry of secondary structure motifs of proteins, and we show how this is consistent with the experimental data. After using the data to universally fix basic local geometric parameters, such as the curvature and torsion of the helical motifs, we are left with a single free parameter. We explain how this parameter controls the abundance and shape of the principal motifs (alpha helices, beta strands and loops connecting them). 1 Introduction Proteins are very complex objects, but in the meantime there is an impressive underlying regularity beyond their structure. This regularity is captured in part by the famous Ramachandran plots that map the correlation of the dihedral (torsion) angles of consecutive bonds in the protein backbone (see for example [1, 2, 3]). The example on figure 1 shows an analogous data of about hundred of proteins, illustrating the localization of the pairs of angles around two regions.1 These two most densely populated regions, labeled α and β, correspond to the most common secondary structure elements in proteins: (right) alpha helices and beta strands.