Mycobacterium tuberculosis Rv2704 is a member of the YjgF/YER057c/UK114 family
Krishan Gopal Thakur
Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
Krishan Gopal Thakur and T. Praveena contributed equally to this work.
Search for more papers by this authorT. Praveena
Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
Krishan Gopal Thakur and T. Praveena contributed equally to this work.
Search for more papers by this authorCorresponding Author
B. Gopal
Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012===Search for more papers by this authorKrishan Gopal Thakur
Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
Krishan Gopal Thakur and T. Praveena contributed equally to this work.
Search for more papers by this authorT. Praveena
Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
Krishan Gopal Thakur and T. Praveena contributed equally to this work.
Search for more papers by this authorCorresponding Author
B. Gopal
Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India
Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012===Search for more papers by this author
Supporting Information
Additional Supporting Information may be found in the online version of this article.
Filename | Description |
---|---|
PROT_22623_sm_suppfig1.tif399 KB | Supplementary Fig. 1. (A) YjgF domains in large multi-domain proteins. An analysis using a limited number of genomic sequences suggested that YjgF proteins do not exist as a domain in multi-domain proteins17. In our analysis with a more updated version of the conserved domain database, we note that there are more than 150 proteins having at least one YjgF domain and ca 100 members having two such domains. The role of these YjgF domains in larger proteins is unclear. The number of known members with a given architecture in the database is listed at the end of each class. (B) Operon analysis. Rv2704 is a part of predicted σA-Rv2704 operon in M. tuberculosis H37Rv. This organization of the σA operon (σA preceding the YjgF homologue) is maintained in some pathogenic mycobacteria like M. ulcerans, M. bovis and M. avium. |
PROT_22623_sm_suppfig2.tif2.4 MB | Supplementary Fig. 2. (A) Structural superimposition of the proposed active site of Rv2704 with five other structural homologs (PDB IDs-1ONI, 2UYN, 2X25, 1QD9, 1QAH). The labels at the top correspond to Rv2704 whereas the labels below correspond to TdcF solved in complex with 2-ketobutyrate (PDB ID 2UYN). Oxygen and carbon atoms of ligand, 2-ketobutyrate, are shown by red and green spheres. Hydrogen bonds are shown by dashed red lines. The side chain of Met100 has not been shown in this figure for clarity. (B) Toplogy diagrams of structural homologs of Rv2704. Topology diagrams were obtained using website PDBsum. Blue arrows indicate the position of helix a1 in Rv2704 and its corresponding structural features in homologue structures. Sequence identities and the RMSDs of the corresponding structures are summarized in supplementary Table I. |
PROT_22623_sm_supptable1.doc53 KB | Supplementary Table I. Structure-Function correlation in YjgF proteins |
Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
REFERENCES
- 1 Ceciliani F,Faotto L,Negri A,Colombo I,Berra B,Bartorelli A,Ronchi S. The primary structure of UK114 tumor antigen. FEBS Lett 1996; 393: 147–150.
- 2 Oka T,Tsuji H,Noda C,Sakai K,Hong YM,Suzuki I,Munoz S,Natori Y. Isolation and characterization of a novel perchloric acid-soluble protein inhibiting cell-free protein synthesis. J Biol Chem 1995; 270: 30060–30067.
- 3 Schmiedeknecht G,Kerkhoff C,Orso E,Stohr J,Aslanidis C,Nagy GM,Knuechel R,Schmitz G. Isolation and characterization of a 14.5-kDa trichloroacetic-acid-soluble translational inhibitor protein from human monocytes that is upregulated upon cellular differentiation. Eur J Biochem 1996; 242: 339–351.
- 4 Morishita R,Kawagoshi A,Sawasaki T,Madin K,Ogasawara T,Oka T,Endo Y. Ribonuclease activity of rat liver perchloric acid-soluble protein, a potent inhibitor of protein synthesis. J Biol Chem 1999; 274: 20688–20692.
- 5 Melloni E,Michetti M,Salamino F,Pontremoli S. Molecular and functional properties of a calpain activator protein specific for mu-isoforms. J Biol Chem 1998; 273: 12827–12831.
- 6 Farkas A,Nardai G,Csermely P,Tompa P,Friedrich P. DUK114, the Drosophila orthologue of bovine brain calpain activator protein, is a molecular chaperone. Biochem J 2004; 383 (Part 1): 165–170.
- 7 Burman JD,Stevenson CE,Sawers RG,Lawson DM. The crystal structure of Escherichia coli TdcF, a member of the highly conserved YjgF/YER057c/UK114 family. BMC Struct Biol 2007; 7: 30.
- 8 Schmitz G,Downs DM. Reduced transaminase B (IlvE) activity caused by the lack of yjgF is dependent on the status of threonine deaminase (IlvA) in Salmonella enterica serovar Typhimurium. J Bacteriol 2004; 186: 803–810.
- 9 Christopherson MR,Schmitz GE,Downs DM. YjgF is required for isoleucine biosynthesis when Salmonella enterica is grown on pyruvate medium. J Bacteriol 2008; 190: 3057–3062.
- 10 Enos-Berlage JL,Langendorf MJ,Downs DM. Complex metabolic phenotypes caused by a mutation in yjgF, encoding a member of the highly conserved YER057c/YjgF family of proteins. J Bacteriol 1998; 180: 6519–6528.
- 11 Kim JM,Yoshikawa H,Shirahige K. A member of the YER057c/yjgf/Uk114 family links isoleucine biosynthesis and intact mitochondria maintenance in Saccharomyces cerevisiae. Genes Cells 2001; 6: 507–517.
- 12 Leitner-Dagan Y,Ovadis M,Zuker A,Shklarman E,Ohad I,Tzfira T,Vainstein A. CHRD, a plant member of the evolutionarily conserved YjgF family, influences photosynthesis and chromoplastogenesis. Planta 2006; 225: 89–102.
- 13 Deaconescu AM,Roll-Mecak A,Bonanno JB,Gerchman SE,Kycia H,Studier FW,Burley SK. X-ray structure of Saccharomyces cerevisiae homologous mitochondrial matrix factor 1 (Hmf1). Proteins 2002; 48: 431–436.
- 14 Deriu D,Briand C,Mistiniene E,Naktinis V,Grutter MG. Structure and oligomeric state of the mammalian tumour-associated antigen UK114. Acta Crystallogr D Biol Crystallogr 2003; 59 (Part 9): 1676–1678.
- 15 Manjasetty BA,Delbruck H,Pham DT,Mueller U,Fieber-Erdmann M,Scheich C,Sievert V,Bussow K,Niesen FH,Weihofen W,Loll B,Saenger W,Heinemann U. Crystal structure of Homo sapiens protein hp14.5. Proteins 2004; 54: 797–800.
- 16 Miyakawa T,Lee WC,Hatano K,Kato Y,Sawano Y,Miyazono K,Nagata K,Tanokura M. Crystal structure of the YjgF/YER057c/UK114 family protein from the hyperthermophilic archaeon Sulfolobus tokodaii strain 7. Proteins 2006; 62: 557–561.
- 17 Sinha S,Rappu P,Lange SC,Mantsala P,Zalkin H,Smith JL. Crystal structure of Bacillus subtilis YabJ, a purine regulatory protein and member of the highly conserved YjgF family. Proc Natl Acad Sci USA 1999; 96: 13074–13079.
- 18 Volz K. A test case for structure-based functional assignment: the 1.2 A crystal structure of the yjgF gene product from Escherichia coli. Protein Sci 1999; 8: 2428–2437.
- 19 Dauter Z,Dauter M. Entering a new phase: using solvent halide ions in protein structure determination. Structure 2001; 9: R21–R26.
- 20 Dauter Z,Dauter M,Rajashankar KR. Novel approach to phasing proteins: derivatization by short cryo-soaking with halides. Acta Crystallogr D Biol Crystallogr 2000; 56 (Part 2): 232–237.
- 21 Mccoy AJ,Grosse-Kunstleve RW,Adams PD,Winn MD,Storoni LC,Read RJ. Phaser crystallographic software. J Appl Crystallogr 2007; 40 (Part 4): 658–674.
- 22 Vagin A,Teplyakov A. MOLREP: an automated program for molecular replacement. J Appl Cryst 1997; 30: 1022–1025.
- 23 Emsley P,Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 2004; 60 (Part 12, Part 1): 2126–2132.
- 24 Murshudov GN,Vagin AA,Dodson EJ. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr 1997; 53 (Part 3): 240–255.
- 25 Dauter M,Dauter Z. Phase determination using halide ions. Methods Mol Biol 2007; 364: 149–158.
- 26 Korolev S,Dementieva I,Sanishvili R,Minor W,Otwinowski Z,Joachimiak A. Using surface-bound rubidium ions for protein phasing. Acta Crystallogr D Biol Crystallogr 2001; 57 (Part 7): 1008–1012.
- 27 Nagem RA,Dauter Z,Polikarpov I. Protein crystal structure solution by fast incorporation of negatively and positively charged anomalous scatterers. Acta Crystallogr D Biol Crystallogr 2001; 57: 996–1002.
- 28 Leslie AGW. Recent changes to the MOSFLM package for processing film and image plate data. Joint CCP4 + ESF-EAMCB Newsletter on Protein Crystallography 1992; 26: 27–33.
- 29 CCP4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 1994; 50 (Part 5): 760–763.
- 30 Cowtan KD,Zhang KY. Density modification for macromolecular phase improvement. Prog Biophys Mol Biol 1999; 72: 245–270.
- 31 Morris RJ,Zwart PH,Cohen S,Fernandez FJ,Kakaris M,Kirillova O,Vonrhein C,Perrakis A,Lamzin VS. Breaking good resolutions with ARP/wARP. J Synchrotron Radiat 2004; 11 (Part 1): 56–59.
- 32 Panjikar S,Parthasarathy V,Lamzin VS,Weiss MS,Tucker PA. Auto-Rickshaw: an automated crystal structure determination platform as an efficient tool for the validation of an X-ray diffraction experiment. Acta Crystallogr D Biol Crystallogr 2005; 61 (Part 4): 449–457.
- 33 Sheldrick GM,Schneider TR. SHELXL: high-resolution refinement. Methods Enzymol 1997; 277: 319–343.
- 34 Terwilliger TC. Maximum-likelihood density modification. Acta Crystallogr D Biol Crystallogr 2000; 56 (Part 8): 965–972.
- 35 Landau M,Mayrose I,Rosenberg Y,Glaser F,Martz E,Pupko T,Ben-Tal N. ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures. Nucleic Acids Res 2005; 33: W299–W302.
- 36 Thompson JD,Higgins DG,Gibson TJ. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994; 22: 4673–4680.
- 37 Gouet P,Courcelle E,Stuart DI,Metoz F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 1999; 15: 305–308.
- 38 Glaser F,Morris RJ,Najmanovich RJ,Laskowski RA,Thornton JM. A method for localizing ligand binding pockets in protein structures. Proteins 2006; 62: 479–488.
- 39 Parsons L,Bonander N,Eisenstein E,Gilson M,Kairys V,Orban J. Solution structure and functional ligand screening of HI0719, a highly conserved protein from bacteria to humans in the YjgF/YER057c/UK114 family. Biochemistry 2003; 42: 80–89.
- 40 Weng M,Nagy PL,Zalkin H. Identification of the Bacillus subtilis pur operon repressor. Proc Natl Acad Sci USA 1995; 92: 7455–7459.