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      Is Open Access

      Every OGT Is Illuminated … by Fluorescent and Synchrotron Lights

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          Abstract

          O 6-DNA-alkyl-guanine-DNA-alkyl-transferases (OGTs) are evolutionarily conserved, unique proteins that repair alkylation lesions in DNA in a single step reaction. Alkylating agents are environmental pollutants as well as by-products of cellular reactions, but are also very effective chemotherapeutic drugs. OGTs are major players in counteracting the effects of such agents, thus their action in turn affects genome integrity, survival of organisms under challenging conditions and response to chemotherapy. Numerous studies on OGTs from eukaryotes, bacteria and archaea have been reported, highlighting amazing features that make OGTs unique proteins in their reaction mechanism as well as post-reaction fate. This review reports recent functional and structural data on two prokaryotic OGTs, from the pathogenic bacterium Mycobacterium tuberculosis and the hyperthermophilic archaeon Sulfolobus solfataricus, respectively. These studies provided insight in the role of OGTs in the biology of these microorganisms, but also important hints useful to understand the general properties of this class of proteins.

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          The green fluorescent protein.

          R Tsien (1998)
          In just three years, the green fluorescent protein (GFP) from the jellyfish Aequorea victoria has vaulted from obscurity to become one of the most widely studied and exploited proteins in biochemistry and cell biology. Its amazing ability to generate a highly visible, efficiently emitting internal fluorophore is both intrinsically fascinating and tremendously valuable. High-resolution crystal structures of GFP offer unprecedented opportunities to understand and manipulate the relation between protein structure and spectroscopic function. GFP has become well established as a marker of gene expression and protein targeting in intact cells and organisms. Mutagenesis and engineering of GFP into chimeric proteins are opening new vistas in physiological indicators, biosensors, and photochemical memories.
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            Genes required for mycobacterial growth defined by high density mutagenesis.

            Christopher Sassetti, Dana Boyd, Eric Rubin (2003)
            Despite over a century of research, tuberculosis remains a leading cause of infectious death worldwide. Faced with increasing rates of drug resistance, the identification of genes that are required for the growth of this organism should provide new targets for the design of antimycobacterial agents. Here, we describe the use of transposon site hybridization (TraSH) to comprehensively identify the genes required by the causative agent, Mycobacterium tuberculosis, for optimal growth. These genes include those that can be assigned to essential pathways as well as many of unknown function. The genes important for the growth of M. tuberculosis are largely conserved in the degenerate genome of the leprosy bacillus, Mycobacterium leprae, indicating that non-essential functions have been selectively lost since this bacterium diverged from other mycobacteria. In contrast, a surprisingly high proportion of these genes lack identifiable orthologues in other bacteria, suggesting that the minimal gene set required for survival varies greatly between organisms with different evolutionary histories.
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              A general method for the covalent labeling of fusion proteins with small molecules in vivo.

              Antje Keppler, Susanne Gendreizig, Thomas Gronemeyer … (2003)
              Characterizing the movement, interactions, and chemical microenvironment of a protein inside the living cell is crucial to a detailed understanding of its function. Most strategies aimed at realizing this objective are based on genetically fusing the protein of interest to a reporter protein that monitors changes in the environment of the coupled protein. Examples include fusions with fluorescent proteins, the yeast two-hybrid system, and split ubiquitin. However, these techniques have various limitations, and considerable effort is being devoted to specific labeling of proteins in vivo with small synthetic molecules capable of probing and modulating their function. These approaches are currently based on the noncovalent binding of a small molecule to a protein, the formation of stable complexes between biarsenical compounds and peptides containing cysteines, or the use of biotin acceptor domains. Here we describe a general method for the covalent labeling of fusion proteins in vivo that complements existing methods for noncovalent labeling of proteins and that may open up new ways of studying proteins in living cells.
              Article 0 comments Cited 466 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (nlm-ta): Int J Mol Sci
                Journal ID (iso-abbrev): Int J Mol Sci
                Journal ID (publisher-id): ijms
                Title: International Journal of Molecular Sciences
                Publisher: MDPI
                ISSN (Electronic): 1422-0067
                Publication date (Electronic): 05 December 2017
                Publication date Collection: December 2017
                Volume: 18
                Issue: 12
                Electronic Location Identifier: 2613
                Affiliations
                [1 ]DSF-Dipartimento di Scienze del Farmaco, University of Piemonte Orientale, Via Bovio 6, 28100 Novara, Italy; riccardo.miggiano@ 123456uniupo.it (R.M.); franca.rossi@ 123456uniupo.it (F.R.); menico.rizzi@ 123456uniupo.it (M.R.)
                [2 ]Institute of Biosciences and BioResources, National Research Council of Italy, Via Pietro Castellino 111, 80131 Naples, Italy; anna.valenti@ 123456ibbr.cnr.it
                Author notes
                [* ]Correspondence: giuseppe.perugino@ 123456ibbr.cnr.it (G.P.); maria.ciaramella@ 123456ibbr.cnr.it (M.C.); Tel.: +39-081-6132-496 (G.P.); +39-081-6132-274 (M.C.); Fax: +39-081-6132-646 (M.C.)
                Article
                Publisher ID: ijms-18-02613
                DOI: 10.3390/ijms18122613
                PMC ID: 5751216
                PubMed ID: 29206193
                SO-VID: 21a30b45-c4ef-40d6-b277-fda0f88de05e
                Copyright © © 2017 by the authors.
                License:

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                Date received : 15 November 2017
                Date accepted : 30 November 2017
                Categories
                Subject: Review

                ScienceOpen disciplines: Molecular biology
                Keywords: dna repair,alkylation damage,conformational changes,protein structure,protein stability,protein-tag
                Data availability:
                ScienceOpen disciplines: Molecular biology
                Keywords: dna repair, alkylation damage, conformational changes, protein structure, protein stability, protein-tag

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