The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

secY  -  preprotein translocase membrane subunit

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK3287, JW3262, prlA
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of secY

  • Escherichia coli prlA mutants (altered in the secY gene) are able to export cell envelope proteins lacking any signal sequence [1].
  • Membrane insertion defects caused by positive charges in the early mature region of protein pIII of filamentous phage fd can be corrected by prlA suppressors [2].
  • The chromosomal region encoding the secY gene of Streptomyces griseus N2-3-11 was cloned and analyzed [3].
  • The secY gene of Vibrio cholerae has been cloned and the complete nt sequence determined [4].
  • A conserved domain of the secY genes from Bacillus subtilis, Mycoplasma capricolum and Escherichia coli was used to design degenerate oligodeoxyribonucleotides [5].

High impact information on secY

  • Evidence from gene fusions constructed in vitro suggests that prlA codes for a protein containing at least 300 amino acids [6].
  • Combinations of certain prlA and prlG mutations, known to cause synthetic lethality in vivo, dramatically loosen subunit association and lead to complete disassembly of SecYEG [7].
  • Since most suppressors of this toxic phenotype map to secA and secY, growth arrest results from a defective interaction of the chimeric protein with the export machinery [8].
  • Suppressor mutations that alter SecY (the prlA alleles) broaden the specificity of this machinery and allow secretion of precursor proteins with defective signal sequences [9].
  • We demonstrate that two exported proteins of E.coli, maltose-binding protein and alkaline phosphatase, each lacking its entire signal sequence, are exported to the periplasm in several prlA mutants [10].

Chemical compound and disease context of secY

  • When expressed from the lac promoter, V. cholerae secY partially complements E. coli secY mutation even in absence of IPTG, while the E. coli secY gene complements only when IPTG is present [4].

Biological context of secY

  • The phenotypes of temperature-sensitive and cold-sensitive mutations in secY suggest that the SecY protein plays an essential role in vivo to facilitate protein translocation, whereas the prlA mutations in this gene suggest that SecY may interact with the signal sequence of translocating polypeptides [11].
  • The E. coli secY (prlA) gene, located in the operator-distal part of the spc ribosomal protein operon, codes for an integral membrane protein, SecY [11].
  • We have now placed the secY, secE, and secG genes under the control of an arabinose-inducible promoter on a multicopy plasmid [12].
  • Some secY mutations, including secY39, interfered with protein export when expressed from a multicopy plasmid, even in the presence of wild-type secY on the chromosome [13].
  • We discuss the mechanism of prlA-mediated export and the role of the protein translocation apparatus in contributing to membrane protein topology [14].

Anatomical context of secY

  • The secY (prlA) gene product is an essential component of the Escherichia coli cytoplasmic membrane, and its function is required for the translocation of exocytoplasmic proteins across the membrane [15].
  • We report here on the retention of a secY gene in cyanelle (= plastid) DNA of the eukaryotic protist Cyanophora paradoxa [16].
  • A processed form of maltose-binding protein (MBP) was detected in the spheroplasts of secY and secA temperature-sensitive mutant cells that had been pulse-labeled at the permissive temperature (30 degrees C) [17].
  • Membranes derived from secY ts cells which were incubated at 42 degrees C were inactive in vitro in the post-translational uptake and processing of pro-OmpA [18].

Associations of secY with chemical compounds

  • The in vivo synthesis and export of plasmid-encoded MBP were studied in the presence and absence of isopropyl thiogalactoside and maltose and in a strain harboring a prlA mutation that suppresses the malE signal sequence mutation and is thought to alter the export machinery of cells [19].
  • In contrast, translocation of these domains was retarded markedly when sodium azide was added to inhibit SecA ATPase and blocked almost completely in secY- or secD-defective mutant cells [20].
  • A combination of this secY mutation and the secG deletion resulted in synthetic lethality, and the TM3 and TM4 SecY cysteine substitution mutations were examined for their ability to complement this lethality [21].
  • Anhydrotetracycline-mediated induction of pKOR1-encoded secY antisense transcripts via the Pxyl/tetO promoter, a condition that is not compatible with staphylococcal growth, selects for chromosomal excision and loss of plasmid [22].

Other interactions of secY

  • The allele-specific synthetic lethality of prlA-prlG double mutants predicts interactive domains of SecY and SecE [23].
  • We also studied the phenotypes of strains in which one of the secY mutations was combined with the components of the secD operon [13].
  • Our evidence indicates that the prlA and prlD gene products play an important role in the normal pathway for export of proteins to the cell envelope [24].
  • We describe in this review recent results focusing on the function of the secA, secB, and secY gene products and the demonstration of their requirement for in vitro protein translocation [25].

Analytical, diagnostic and therapeutic context of secY


  1. Targeting of signal sequenceless proteins for export in Escherichia coli with altered protein translocase. Prinz, W.A., Spiess, C., Ehrmann, M., Schierle, C., Beckwith, J. EMBO J. (1996) [Pubmed]
  2. Membrane insertion defects caused by positive charges in the early mature region of protein pIII of filamentous phage fd can be corrected by prlA suppressors. Peters, E.A., Schatz, P.J., Johnson, S.S., Dower, W.J. J. Bacteriol. (1994) [Pubmed]
  3. Analysis and regulation of the secY gene(1) from Streptomyces griseus N2-3-11 and interaction of the SecY protein with the SecA protein. Pöhling, S., Piepersberg, W., Wehmeier, U.F. Biochim. Biophys. Acta (1999) [Pubmed]
  4. The secY gene of V. cholerae: identification, cloning and characterization. Bhattacharyya, D., Das, J. Gene (1997) [Pubmed]
  5. Cloning and sequencing of the secY homolog from Coryneform bacteria. Kobayashi, M., Fugono, N., Asai, Y., Inui, M., Vertès, A.A., Kurusu, Y., Yukawa, H. Gene (1994) [Pubmed]
  6. A previously unidentified gene in the spc operon of Escherichia coli K12 specifies a component of the protein export machinery. Shultz, J., Silhavy, T.J., Berman, M.L., Fiil, N., Emr, S.D. Cell (1982) [Pubmed]
  7. The PrlA and PrlG phenotypes are caused by a loosened association among the translocase SecYEG subunits. Duong, F., Wickner, W. EMBO J. (1999) [Pubmed]
  8. A new genetic selection identifies essential residues in SecG, a component of the Escherichia coli protein export machinery. Bost, S., Belin, D. EMBO J. (1995) [Pubmed]
  9. PrlA suppressor mutations cluster in regions corresponding to three distinct topological domains. Osborne, R.S., Silhavy, T.J. EMBO J. (1993) [Pubmed]
  10. A signal sequence is not required for protein export in prlA mutants of Escherichia coli. Derman, A.I., Puziss, J.W., Bassford, P.J., Beckwith, J. EMBO J. (1993) [Pubmed]
  11. Structure, function, and biogenesis of SecY, an integral membrane protein involved in protein export. Ito, K. J. Bioenerg. Biomembr. (1990) [Pubmed]
  12. SecYEG and SecA are the stoichiometric components of preprotein translocase. Douville, K., Price, A., Eichler, J., Economou, A., Wickner, W. J. Biol. Chem. (1995) [Pubmed]
  13. Genetic analysis of SecY: additional export-defective mutations and factors affecting their phenotypes. Taura, T., Akiyama, Y., Ito, K. Mol. Gen. Genet. (1994) [Pubmed]
  14. The protein translocation apparatus contributes to determining the topology of an integral membrane protein in Escherichia coli. Prinz, W.A., Boyd, D.H., Ehrmann, M., Beckwith, J. J. Biol. Chem. (1998) [Pubmed]
  15. Topology analysis of the SecY protein, an integral membrane protein involved in protein export in Escherichia coli. Akiyama, Y., Ito, K. EMBO J. (1987) [Pubmed]
  16. SecY, an integral subunit of the bacterial preprotein translocase, is encoded by a plastid genome. Flachmann, R., Michalowski, C.B., Löffelhardt, W., Bohnert, H.J. J. Biol. Chem. (1993) [Pubmed]
  17. Escherichia coli sec mutants accumulate a processed immature form of maltose-binding protein (MBP), a late-phase intermediate in MBP export. Ueguchi, C., Ito, K. J. Bacteriol. (1990) [Pubmed]
  18. The secY protein can act post-translationally to promote bacterial protein export. Bacallao, R., Crooke, E., Shiba, K., Wickner, W., Ito, K. J. Biol. Chem. (1986) [Pubmed]
  19. In vivo and in vitro synthesis of Escherichia coli maltose-binding protein under regulatory control of the lacUV5 promoter-operator. Rasmussen, B.A., MacGregor, C.H., Ray, P.H., Bassford, P.J. J. Bacteriol. (1985) [Pubmed]
  20. Translocation, folding, and stability of the HflKC complex with signal anchor topogenic sequences. Kihara, A., Ito, K. J. Biol. Chem. (1998) [Pubmed]
  21. Mutational analysis of transmembrane regions 3 and 4 of SecY, a central component of protein translocase. Mori, H., Shimokawa, N., Satoh, Y., Ito, K. J. Bacteriol. (2004) [Pubmed]
  22. Allelic replacement in Staphylococcus aureus with inducible counter-selection. Bae, T., Schneewind, O. Plasmid (2006) [Pubmed]
  23. The allele-specific synthetic lethality of prlA-prlG double mutants predicts interactive domains of SecY and SecE. Flower, A.M., Osborne, R.S., Silhavy, T.J. EMBO J. (1995) [Pubmed]
  24. Proper interaction between at least two components is required for efficient export of proteins to the Escherichia coli cell envelope. Bankaitis, V.A., Bassford, P.J. J. Bacteriol. (1985) [Pubmed]
  25. Protein translocation in vitro: biochemical characterization of genetically defined translocation components. Fandl, J., Tai, P.C. J. Bioenerg. Biomembr. (1990) [Pubmed]
  26. Isolation and analysis of novel mutants of Escherichia coli prlA (secY). Olsen, M.K., Rosey, E.L., Tomich, C.S. J. Bacteriol. (1993) [Pubmed]
  27. The RNA polymerase alpha subunit from Sinorhizobium meliloti can assemble with RNA polymerase subunits from Escherichia coli and function in basal and activated transcription both in vivo and in vitro. Peck, M.C., Gaal, T., Fisher, R.F., Gourse, R.L., Long, S.R. J. Bacteriol. (2002) [Pubmed]
WikiGenes - Universities