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Gene Review

secE  -  preprotein translocase membrane subunit

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK3972, JW3944, mbrC, prlG
 
 
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Disease relevance of secE

  • The data presented here and in the accompanying paper strongly suggest that secE has an important role in E. coli protein export [1].
  • Isolation and characterization of the secE homologue gene of Bacillus subtilis [2].
  • Study of the five Rickettsia prowazekii proteins annotated as ATP/ADP translocases (Tlc): Only Tlc1 transports ATP/ADP, while Tlc4 and Tlc5 transport other ribonucleotides [3].
  • The molecular target for the bacteriolytic E protein from bacteriophage X174, responsible for host cell lysis, is known to be the enzyme phospho-MurNAc-pentapeptide translocase (MraY), an integral membrane protein involved in bacterial cell wall peptidoglycan biosynthesis, with an essential role being played by peptidyl-prolyl isomerase SlyD [4].
 

High impact information on secE

  • In contrast, mutations at mbrB, mbrC, and mbrD exhibit their phenotypes independent of oriC initiation of DNA replication, suggesting that the mutations affect factors that influence the DNA/cell ratio regardless of the origin of DNA replication [5].
  • FtsK is a DNA translocase that coordinates chromosome segregation and cell division in bacteria [6].
  • (i) Formaldehyde cross- linking of translocase reveals cross-links between SecY, SecE and SecG, but not higher order oligomers [7].
  • 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 [8].
  • A deletion of nearly the entire gene renders the cell dependent on the presence of a complementing secE+ plasmid, indicating that the SecE protein is essential for growth [9].
 

Chemical compound and disease context of secE

  • Affinity of TatCd for TatAd elucidates its receptor function in the Bacillus subtilis twin arginine translocation (Tat) translocase system [10].
  • The Rickettsia prowazekii ATP/ADP translocase was identified by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE) and immunoblot analysis using antibodies raised against a synthetic peptide corresponding in sequence to the carboxyl-terminal 17 amino acids of the carrier [11].
  • Similar concentrations of disulfide bond-reducing agents inhibited the exchange transport of adenine nucleotides by both R. prowazekii and translocase-expressing E. coli [11].
 

Biological context of secE

 

Anatomical context of secE

 

Associations of secE with chemical compounds

  • The paradigm for the study of rickettsial transport systems is the ATP/ADP translocase Tlc1, which exchanges bacterial ADP for host cell ATP as a source of energy, rather than as a source of adenylate [3].
  • Cysteine-scanning Mutagenesis and Disulfide Mapping Studies of the Conserved Domain of the Twin-arginine Translocase TatB Component [18].
  • We have previously identified 20 different fusidic acid-resistant alleles of fusA, encoding mutant forms of the ribosomal translocase EF-G [19].
  • They include three isoforms of the ADP/ATP translocase and the phosphate and citrate carriers [20].
  • Interplay of the Wzx translocase and the corresponding polymerase and chain length regulator proteins in the translocation and periplasmic assembly of lipopolysaccharide o antigen [21].
 

Other interactions of secE

  • The secE-nusG genes are cotranscribed, with transcripts initiated at the PEG promoter and terminated at the Rho-independent terminator in the region of the rplK promoter [13].
 

Analytical, diagnostic and therapeutic context of secE

  • Both the translocase of R. prowazekii and that expressed by Escherichia coli transformants containing the rickettsial gene had an apparent molecular mass of 36,500 Da by SDS-PAGE analysis, a mass considerably less than that deduced from the sequence of the gene [11].

References

  1. The secE gene encodes an integral membrane protein required for protein export in Escherichia coli. Schatz, P.J., Riggs, P.D., Jacq, A., Fath, M.J., Beckwith, J. Genes Dev. (1989) [Pubmed]
  2. Isolation and characterization of the secE homologue gene of Bacillus subtilis. Jeong, S.M., Yoshikawa, H., Takahashi, H. Mol. Microbiol. (1993) [Pubmed]
  3. Study of the five Rickettsia prowazekii proteins annotated as ATP/ADP translocases (Tlc): Only Tlc1 transports ATP/ADP, while Tlc4 and Tlc5 transport other ribonucleotides. Audia, J.P., Winkler, H.H. J. Bacteriol. (2006) [Pubmed]
  4. Interaction of the transmembrane domain of lysis protein E from bacteriophage {phi}X174 with bacterial translocase MraY and peptidyl-prolyl isomerase SlyD. Mendel, S., Holbourn, J.M., Schouten, J.A., Bugg, T.D. Microbiology (Reading, Engl.) (2006) [Pubmed]
  5. On the bacterial cell cycle: Escherichia coli mutants with altered ploidy. Trun, N.J., Gottesman, S. Genes Dev. (1990) [Pubmed]
  6. Double-stranded DNA translocation: structure and mechanism of hexameric FtsK. Massey, T.H., Mercogliano, C.P., Yates, J., Sherratt, D.J., Löwe, J. Mol. Cell (2006) [Pubmed]
  7. Evaluating the oligomeric state of SecYEG in preprotein translocase. Yahr, T.L., Wickner, W.T. EMBO J. (2000) [Pubmed]
  8. The PrlA and PrlG phenotypes are caused by a loosened association among the translocase SecYEG subunits. Duong, F., Wickner, W. EMBO J. (1999) [Pubmed]
  9. One of three transmembrane stretches is sufficient for the functioning of the SecE protein, a membrane component of the E. coli secretion machinery. Schatz, P.J., Bieker, K.L., Ottemann, K.M., Silhavy, T.J., Beckwith, J. EMBO J. (1991) [Pubmed]
  10. Affinity of TatCd for TatAd elucidates its receptor function in the Bacillus subtilis twin arginine translocation (Tat) translocase system. Schreiber, S., Stengel, R., Westermann, M., Volkmer-Engert, R., Pop, O.I., Müller, J.P. J. Biol. Chem. (2006) [Pubmed]
  11. Identification and initial topological analysis of the Rickettsia prowazekii ATP/ADP translocase. Plano, G.V., Winkler, H.H. J. Bacteriol. (1991) [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. Sequence and transcriptional pattern of the essential Escherichia coli secE-nusG operon. Downing, W.L., Sullivan, S.L., Gottesman, M.E., Dennis, P.P. J. Bacteriol. (1990) [Pubmed]
  14. 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]
  15. Genetic dissection of SecA: suppressor mutations against the secY205 translocase defect. Matsumoto, G., Nakatogawa, H., Mori, H., Ito, K. Genes Cells (2000) [Pubmed]
  16. Distribution of binding sequences for the mitochondrial import receptors Tom20, Tom22, and Tom70 in a presequence-carrying preprotein and a non-cleavable preprotein. Brix, J., Rüdiger, S., Bukau, B., Schneider-Mergener, J., Pfanner, N. J. Biol. Chem. (1999) [Pubmed]
  17. Solubilization and reconstitution of the Rickettsia prowazekii ATP/ADP translocase. Plano, G.V., Winkler, H.H. J. Membr. Biol. (1989) [Pubmed]
  18. Cysteine-scanning Mutagenesis and Disulfide Mapping Studies of the Conserved Domain of the Twin-arginine Translocase TatB Component. Lee, P.A., Orriss, G.L., Buchanan, G., Greene, N.P., Bond, P.J., Punginelli, C., Jack, R.L., Sansom, M.S., Berks, B.C., Palmer, T. J. Biol. Chem. (2006) [Pubmed]
  19. The dynamic structure of EF-G studied by fusidic acid resistance and internal revertants. Johanson, U., Aevarsson, A., Liljas, A., Hughes, D. J. Mol. Biol. (1996) [Pubmed]
  20. Yeast mitochondrial carriers: bacterial expression, biochemical identification and metabolic significance. Palmieri, L., Runswick, M.J., Fiermonte, G., Walker, J.E., Palmieri, F. J. Bioenerg. Biomembr. (2000) [Pubmed]
  21. Interplay of the Wzx translocase and the corresponding polymerase and chain length regulator proteins in the translocation and periplasmic assembly of lipopolysaccharide o antigen. Marolda, C.L., Tatar, L.D., Alaimo, C., Aebi, M., Valvano, M.A. J. Bacteriol. (2006) [Pubmed]
 
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