slyD

Summary

Gene Symbol: slyD
Description: FKBP-type peptidyl prolyl cis-trans isomerase (rotamase)
Alias: ECK3336, JW3311
Species: Escherichia coli str. K-12 substr. MG1655
Products:     slyD

Top Publications

  1. Hottenrott S, Schumann T, Pl ckthun A, Fischer G, Rahfeld J. The Escherichia coli SlyD is a metal ion-regulated peptidyl-prolyl cis/trans-isomerase. J Biol Chem. 1997;272:15697-701 pubmed
    ..However, for three of them, the histidine-rich SlyD, the homologous gene product of ORF149, and parvulin-like SurA, it was not known whether these proteins really ..
  2. Zhang J, Butland G, Greenblatt J, Emili A, Zamble D. A role for SlyD in the Escherichia coli hydrogenase biosynthetic pathway. J Biol Chem. 2005;280:4360-6 pubmed
    ..The analysis of the proteins in a complex with HypB revealed the peptidyl-prolyl cis/trans-isomerase SlyD, a metal-binding protein that has not been previously linked to the hydrogenase biosynthetic pathway...
  3. Roof W, Horne S, Young K, Young R. slyD, a host gene required for phi X174 lysis, is related to the FK506-binding protein family of peptidyl-prolyl cis-trans-isomerases. J Biol Chem. 1994;269:2902-10 pubmed
    Recessive mutations in the slyD gene were isolated by selecting for survival after induction of the cloned lysis gene E of bacteriophage phi X174 (Maratea, D., Young, K., and Young, R. (1985) Gene (Amst.) 40, 39-46)...
  4. Scholz C, Eckert B, Hagn F, Schaarschmidt P, Balbach J, Schmid F. SlyD proteins from different species exhibit high prolyl isomerase and chaperone activities. Biochemistry. 2006;45:20-33 pubmed
    b>SlyD is a putative folding helper protein from the Escherichia coli cytosol, which consists of an N-terminal prolyl isomerase domain of the FKBP type and a presumably unstructured C-terminal tail...
  5. Maratea D, Young K, Young R. Deletion and fusion analysis of the phage phi X174 lysis gene E. Gene. 1985;40:39-46 pubmed
    ..The lethal E phi lacZ fusions are also lethal to a mutant, designated slyD, which was isolated as a spontaneous E. coli mutant resistant to the expression of the intact E gene...
  6. Bernhardt T, Roof W, Young R. The Escherichia coli FKBP-type PPIase SlyD is required for the stabilization of the E lysis protein of bacteriophage phi X174. Mol Microbiol. 2002;45:99-108 pubmed
    ..Recessive mutations in the host gene slyD (sensitivity to lysis) absolutely block E-mediated lysis and phi X174 plaque formation...
  7. Kaluarachchi H, Sutherland D, Young A, Pickering I, Stillman M, Zamble D. The Ni(II)-binding properties of the metallochaperone SlyD. J Am Chem Soc. 2009;131:18489-500 pubmed publisher
    ..In this study we examine the nickel-binding properties of the Escherichia coli protein SlyD, a factor that contributes to optimal nickel accumulation in this organism. This protein is also required for E...
  8. Pinske C, Sargent F, Sawers R. SlyD-dependent nickel delivery limits maturation of [NiFe]-hydrogenases in late-stationary phase Escherichia coli cells. Metallomics. 2015;7:683-90 pubmed publisher
    ..the insertion of a Fe(CN)2CO group and a subsequent insertion of nickel ions through the HypA/HybF, HypB and SlyD proteins...
  9. Mitterauer T, Nanoff C, Ahorn H, Freissmuth M, Hohenegger M. Metal-dependent nucleotide binding to the Escherichia coli rotamase SlyD. Biochem J. 1999;342 ( Pt 1):33-9 pubmed
    ..and 2',3'-dialdehyde-ATP); the protein was purified separately and identified as Escherichia coli SlyD by N-terminal amino acid sequence determination. SlyD is the host protein required for lysis of E...

More Information

Publications41

  1. Chan Chung K, Zamble D. Protein interactions and localization of the Escherichia coli accessory protein HypA during nickel insertion to [NiFe] hydrogenase. J Biol Chem. 2011;286:43081-90 pubmed publisher
    ..delivery during maturation of Escherichia coli [NiFe] hydrogenase 3 includes the accessory proteins HypA, HypB, and SlyD. Although the isolated proteins have been characterized, little is known about how they interact with each other ..
  2. Bernhardt T, Roof W, Young R. Genetic evidence that the bacteriophage phi X174 lysis protein inhibits cell wall synthesis. Proc Natl Acad Sci U S A. 2000;97:4297-302 pubmed
    ..In a search for the cellular target of E, we previously have isolated recessive mutations in the host gene slyD (sensitivity to lysis) that block the lytic effects of E...
  3. Gerard M, Debyser Z, Desender L, Kahle P, Baert J, Baekelandt V, et al. The aggregation of alpha-synuclein is stimulated by FK506 binding proteins as shown by fluorescence correlation spectroscopy. FASEB J. 2006;20:524-6 pubmed
    ..This effect was observed both with E. coli SlyD FKBP and with human FKBP12 and was counteracted by FK506, a specific inhibitor of FKBP...
  4. Horne S, Young K. Escherichia coli and other species of the Enterobacteriaceae encode a protein similar to the family of Mip-like FK506-binding proteins. Arch Microbiol. 1995;163:357-65 pubmed
    ..Thus, mip-like genes are not found exclusively in bacteria having a predominately intracellular life style, but instead appear to be a new FKBP subfamily that is a common constituent of many bacteria. ..
  5. Amitai S, Kolodkin Gal I, Hananya Meltabashi M, Sacher A, Engelberg Kulka H. Escherichia coli MazF leads to the simultaneous selective synthesis of both "death proteins" and "survival proteins". PLoS Genet. 2009;5:e1000390 pubmed publisher
  6. Wulfing C, Lombardero J, Pluckthun A. An Escherichia coli protein consisting of a domain homologous to FK506-binding proteins (FKBP) and a new metal binding motif. J Biol Chem. 1994;269:2895-901 pubmed
    ..The protein binds Ni2+ and Zn2+ tightly with 1:1 stoichiometry, Cu2+ and Co2+ with lower affinity, and Mn2+, Fe2+, Fe3+, Mg2+, and Ca2+ hardly at all. ..
  7. Yan S, Beeler J, Chen Y, Shelton R, Tang W. The regulation of type 7 adenylyl cyclase by its C1b region and Escherichia coli peptidylprolyl isomerase, SlyD. J Biol Chem. 2001;276:8500-6 pubmed
    ..The C1a, C1b, and C2a domains of AC7 were purified separately. Escherichia coli SlyD protein, a cis-trans peptidylprolyl isomerase (PPIase), copurifies with AC7 C1b (7C1b)...
  8. Knappe T, Eckert B, Schaarschmidt P, Scholz C, Schmid F. Insertion of a chaperone domain converts FKBP12 into a powerful catalyst of protein folding. J Mol Biol. 2007;368:1458-68 pubmed
    ..In contrast, the SlyD proteins, which are members of the FKBP family, are highly active as folding enzymes...
  9. Weininger U, Haupt C, Schweimer K, Graubner W, Kovermann M, Brüser T, et al. NMR solution structure of SlyD from Escherichia coli: spatial separation of prolyl isomerase and chaperone function. J Mol Biol. 2009;387:295-305 pubmed publisher
    b>SlyD (sensitive to lysis D) is a putative folding helper from the bacterial cytosol and harbors prolyl isomerase and chaperone activities...
  10. Kaluarachchi H, Altenstein M, Sugumar S, Balbach J, Zamble D, Haupt C. Nickel binding and [NiFe]-hydrogenase maturation by the metallochaperone SlyD with a single metal-binding site in Escherichia coli. J Mol Biol. 2012;417:28-35 pubmed publisher
    b>SlyD (sensitive to lysis D) is a nickel metallochaperone involved in the maturation of [NiFe]-hydrogenases in Escherichia coli (E. coli) and specifically contributes to the nickel delivery step during enzyme biosynthesis...
  11. Parsy C, Chapman C, Barnes A, Robertson J, Murray A. Two-step method to isolate target recombinant protein from co-purified bacterial contaminant SlyD after immobilised metal affinity chromatography. J Chromatogr B Analyt Technol Biomed Life Sci. 2007;853:314-9 pubmed
    ..recombinant expression, through metal immobilised affinity chromatography (IMAC), we encountered a contaminant, SlyD, a 29 kDa native E. coli protein...
  12. Zoldak G, Schmid F. Cooperation of the prolyl isomerase and chaperone activities of the protein folding catalyst SlyD. J Mol Biol. 2011;406:176-94 pubmed publisher
    The SlyD (sensitive to lysis D) protein of Escherichia coli is a folding enzyme with a chaperone domain and a prolyl isomerase domain of the FK506 binding protein type...
  13. Zhang J, Leach M, Zamble D. The peptidyl-prolyl isomerase activity of SlyD is not required for maturation of Escherichia coli hydrogenase. J Bacteriol. 2007;189:7942-4 pubmed
    Escherichia coli SlyD, which is involved in the biosynthesis of the metal cluster in the [NiFe]-hydrogenase enzymes, exhibits several activities including that of a peptidyl-prolyl isomerase (PPIase)...
  14. Jakob R, Zoldak G, Aumüller T, Schmid F. Chaperone domains convert prolyl isomerases into generic catalysts of protein folding. Proc Natl Acad Sci U S A. 2009;106:20282-7 pubmed publisher
    ..Several prolyl isomerases of the FK506-binding protein family, such as trigger factor, SlyD, and FkpA, contain chaperone domains and are assumed to assist protein folding in vivo...
  15. Zoldak G, Aumüller T, Lücke C, Hritz J, Oostenbrink C, Fischer G, et al. A library of fluorescent peptides for exploring the substrate specificities of prolyl isomerases. Biochemistry. 2009;48:10423-36 pubmed publisher
    ..In a second application, the substrate specificity of SlyD, a protease-sensitive prolyl isomerase from Escherichia coli, was characterized and compared with that of human ..
  16. Rosenberg S. Life, death, differentiation, and the multicellularity of bacteria. PLoS Genet. 2009;5:e1000418 pubmed publisher
  17. Mukherjee S, Shukla A, Guptasarma P. Single-step purification of a protein-folding catalyst, the SlyD peptidyl prolyl isomerase (PPI), from cytoplasmic extracts of Escherichia coli. Biotechnol Appl Biochem. 2003;37:183-6 pubmed
    The protein-folding catalyst SlyD, a peptidyl prolyl cis-trans isomerase regulated by metal binding, was initially discovered as a major contaminant of non-denaturing immobilized metal-affinity chromatography (IMAC)-based procedures for ..
  18. Janowski B, Wollner S, Schutkowski M, Fischer G. A protease-free assay for peptidyl prolyl cis/trans isomerases using standard peptide substrates. Anal Biochem. 1997;252:299-307 pubmed
    ..constants of cytosolic cyclophilin (Cyp18) and of the proteolytically sensitive FK506-binding protein-like PPIase SlyD from Escherichia coli...
  19. Roof W, Fang H, Young K, Sun J, Young R. Mutational analysis of slyD, an Escherichia coli gene encoding a protein of the FKBP immunophilin family. Mol Microbiol. 1997;25:1031-46 pubmed
    b>slyD encodes a 196 amino acid polypeptide that is a member of the FKBP family of cis-trans peptidyl-prolyl isomerases (PPlases)...
  20. Leach M, Zhang J, Zamble D. The role of complex formation between the Escherichia coli hydrogenase accessory factors HypB and SlyD. J Biol Chem. 2007;282:16177-86 pubmed
    The Escherichia coli protein SlyD is a member of the FK-506-binding protein family of peptidylprolyl isomerases...
  21. Kaluarachchi H, Siebel J, Kaluarachchi Duffy S, Krecisz S, Sutherland D, Stillman M, et al. Metal selectivity of the Escherichia coli nickel metallochaperone, SlyD. Biochemistry. 2011;50:10666-77 pubmed publisher
    b>SlyD is a Ni(II)-binding protein that contributes to nickel homeostasis in Escherichia coli...
  22. Butland G, Zhang J, Yang W, Sheung A, Wong P, Greenblatt J, et al. Interactions of the Escherichia coli hydrogenase biosynthetic proteins: HybG complex formation. FEBS Lett. 2006;580:677-81 pubmed
    ..The complex also includes HypE and HypD, which interact with each other before joining the larger complex. ..
  23. Martino L, Kelly G, Conte M. Letter to the Editor: resonance assignment of SlyD from E. coli. Biomol NMR Assign. 2009;3:235-7 pubmed publisher
    b>SlyD from Escherichia coli is a peptidyl-prolyl cis-trans isomerase involved in [Ni-Fe] hydrogenase metallocentre assembly in bacteria. We present here the backbone and side chain assignments for E. coli SlyD.
  24. Han K, Song J, Ahn K, Park J, Seo H, Lee J. Solubilization of aggregation-prone heterologous proteins by covalent fusion of stress-responsive Escherichia coli protein, SlyD. Protein Eng Des Sel. 2007;20:543-9 pubmed
    ..electrophoresis (2-DE), wherein we identified a FKBP-type peptidyl-prolyl cis-trans isomerse (PPIases), SlyD, as a stress-responsive (i.e. aggregation-resistant) protein...
  25. Kaluarachchi H, Zhang J, Zamble D. Escherichia coli SlyD, more than a Ni(II) reservoir. Biochemistry. 2011;50:10761-3 pubmed publisher
    b>SlyD interacts with HypB and contributes to nickel insertion during [NiFe]-hydrogenase biogenesis...
  26. Graubner W, Schierhorn A, Brüser T. DnaK plays a pivotal role in Tat targeting of CueO and functions beside SlyD as a general Tat signal binding chaperone. J Biol Chem. 2007;282:7116-24 pubmed
    ..Here we show that the chaperones SlyD and DnaK bind to a broad range of different Tat signal sequences in vitro and in vivo...
  27. Yawn B, Zhang L, Mura C, Sukhodolets M. RapA, the SWI/SNF subunit of Escherichia coli RNA polymerase, promotes the release of nascent RNA from transcription complexes. Biochemistry. 2009;48:7794-806 pubmed publisher
    ..In this study, we introduced a model system for in vitro transcription of a full-length Escherichia coli gene (slyD)...
  28. Martino L, He Y, Hands Taylor K, Valentine E, Kelly G, Giancola C, et al. The interaction of the Escherichia coli protein SlyD with nickel ions illuminates the mechanism of regulation of its peptidyl-prolyl isomerase activity. FEBS J. 2009;276:4529-44 pubmed publisher
    The sensitive to lysis D (SlyD) protein from Escherichia coli is related to the FK506-binding protein family, and it harbours both peptidyl-prolyl cis-trans isomerase (PPIase) and chaperone-like activity, preventing aggregation and ..
  29. Zoldak G, Carstensen L, Scholz C, Schmid F. Consequences of domain insertion on the stability and folding mechanism of a protein. J Mol Biol. 2009;386:1138-52 pubmed publisher
    b>SlyD, the sensitive-to-lysis protein from Escherichia coli, consists of two domains...
  30. Bolanos Garcia V, Davies O. Structural analysis and classification of native proteins from E. coli commonly co-purified by immobilised metal affinity chromatography. Biochim Biophys Acta. 2006;1760:1304-13 pubmed
    ..coli most commonly co-purified by IMAC, including Fur, Crp, ArgE, SlyD, GlmS, GlgA, ODO1, ODO2, YadF and YfbG...
  31. Mendel S, Holbourn J, Schouten J, Bugg T. Interaction of the transmembrane domain of lysis protein E from bacteriophage phiX174 with bacterial translocase MraY and peptidyl-prolyl isomerase SlyD. Microbiology. 2006;152:2959-67 pubmed
    ..in bacterial cell wall peptidoglycan biosynthesis, with an essential role being played by peptidyl-prolyl isomerase SlyD. A synthetic 37 aa peptide E(pep), containing the N-terminal transmembrane alpha-helix of E, was found to be ..
  32. Chung K, Zamble D. The Escherichia coli metal-binding chaperone SlyD interacts with the large subunit of [NiFe]-hydrogenase 3. FEBS Lett. 2011;585:291-4 pubmed publisher
    ..A complex with SlyD, a chaperone protein implicated in hydrogenase production through association with the nickel-binding accessory ..