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Pathway Description
Operon: tRNA Synthetase & Peptidase
Escherichia coli
Category:
Metabolite Pathway
Sub-Category:
Signaling
Created: 2015-09-08
Last Updated: 2025-05-10
The ribF-ileS-lspA-fkpB-ispH operon in E. coli contains five genes that encode for various proteins. There are currently no known activators and repressors of this operon.
The first gene, ribF, encodes for a bifunctional riboflavin kinase and FMN adenylyltransferase. In the cell, it is used to convert riboflavin to FMN, and then FMN to FAD.
The second gene, ileS, encodes the isoleucine tRNA ligase or synthetase, which catalyzes the attachment of the amimno acid isoleucine onto its tRNA, forming a charged tRNA.
The third gene, lspA, encodes a lipoprotein signal peptidase. This protein cleaves signal peptides from prolipoproteins, forming the mature lipoprotein, as well as a free signal peptide which is then degraded.
The fourth gene, fkpB, encodes a peptidyl-prolyl cis-trans isomerase which works as an isomerase, and also posesses a chaperone activity, assisting in the folding of several ribosomal proteins.
The final gene, ispH, encodes 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) reductase. This protein catalyzes the conversion of HMBPP into both dimethylallyl diphosphate (DMAPP) and isopentenyl diphosphate (IPP) as part of the methylerythritol phosphate pathway involved in isoprenoid biosynthesis.
References
Operon: tRNA Synthetase & Peptidase References
Kamio Y, Lin CK, Regue M, Wu HC: Characterization of the ileS-lsp operon in Escherichia coli. Identification of an open reading frame upstream of the ileS gene and potential promoter(s) for the ileS-lsp operon. J Biol Chem. 1985 May 10;260(9):5616-20.
Pubmed: 2985604
Goh S, Hohmeier A, Stone TC, Offord V, Sarabia F, Garcia-Ruiz C, Good L: Silencing of Essential Genes within a Highly Coordinated Operon in Escherichia coli. Appl Environ Microbiol. 2015 Aug 15;81(16):5650-9. doi: 10.1128/AEM.01444-15. Epub 2015 Jun 12.
Pubmed: 26070674
Ross, W., Vrentas, C.E., Sanchez-Vazquez, P., Gaal, T. and Gourse, R.L., 2013. The magic spot: a ppGpp binding site on E. coli RNA polymerase responsible for regulation of transcription initiation. Molecular cell, 50(3), pp.420-429.
Zuo, Y., Wang, Y. and Steitz, T.A., 2013. The mechanism of E. coli RNA polymerase regulation by ppGpp is suggested by the structure of their complex. Molecular cell, 50(3), pp.430-436.
Yura T, Mori H, Nagai H, Nagata T, Ishihama A, Fujita N, Isono K, Mizobuchi K, Nakata A: Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region. Nucleic Acids Res. 1992 Jul 11;20(13):3305-8. doi: 10.1093/nar/20.13.3305.
Pubmed: 1630901
Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. doi: 10.1126/science.277.5331.1453.
Pubmed: 9278503
Webster T, Tsai H, Kula M, Mackie GA, Schimmel P: Specific sequence homology and three-dimensional structure of an aminoacyl transfer RNA synthetase. Science. 1984 Dec 14;226(4680):1315-7. doi: 10.1126/science.6390679.
Pubmed: 6390679
Yanagisawa T, Lee JT, Wu HC, Kawakami M: Relationship of protein structure of isoleucyl-tRNA synthetase with pseudomonic acid resistance of Escherichia coli. A proposed mode of action of pseudomonic acid as an inhibitor of isoleucyl-tRNA synthetase. J Biol Chem. 1994 Sep 30;269(39):24304-9.
Pubmed: 7929087
Yu F, Yamada H, Daishima K, Mizushima S: Nucleotide sequence of the lspA gene, the structural gene for lipoprotein signal peptidase of Escherichia coli. FEBS Lett. 1984 Jul 23;173(1):264-8. doi: 10.1016/0014-5793(84)81060-1.
Pubmed: 6378662
Innis MA, Tokunaga M, Williams ME, Loranger JM, Chang SY, Chang S, Wu HC: Nucleotide sequence of the Escherichia coli prolipoprotein signal peptidase (lsp) gene. Proc Natl Acad Sci U S A. 1984 Jun;81(12):3708-12. doi: 10.1073/pnas.81.12.3708.
Pubmed: 6374664
Bouvier J, Stragier P: Nucleotide sequence of the lsp-dapB interval in Escherichia coli. Nucleic Acids Res. 1991 Jan 11;19(1):180. doi: 10.1093/nar/19.1.180.
Pubmed: 2011499
Wolff M, Seemann M, Tse Sum Bui B, Frapart Y, Tritsch D, Garcia Estrabot A, Rodriguez-Concepcion M, Boronat A, Marquet A, Rohmer M: Isoprenoid biosynthesis via the methylerythritol phosphate pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate reductase (LytB/IspH) from Escherichia coli is a [4Fe-4S] protein. FEBS Lett. 2003 Apr 24;541(1-3):115-20. doi: 10.1016/s0014-5793(03)00317-x.
Pubmed: 12706830
Rohdich F, Hecht S, Gartner K, Adam P, Krieger C, Amslinger S, Arigoni D, Bacher A, Eisenreich W: Studies on the nonmevalonate terpene biosynthetic pathway: metabolic role of IspH (LytB) protein. Proc Natl Acad Sci U S A. 2002 Feb 5;99(3):1158-63. doi: 10.1073/pnas.032658999. Epub 2002 Jan 29.
Pubmed: 11818558
Tanaka K, Takayanagi Y, Fujita N, Ishihama A, Takahashi H: Heterogeneity of the principal sigma factor in Escherichia coli: the rpoS gene product, sigma 38, is a second principal sigma factor of RNA polymerase in stationary-phase Escherichia coli. Proc Natl Acad Sci U S A. 1993 Apr 15;90(8):3511-5. doi: 10.1073/pnas.90.8.3511.
Pubmed: 8475100
Mulvey MR, Loewen PC: Nucleotide sequence of katF of Escherichia coli suggests KatF protein is a novel sigma transcription factor. Nucleic Acids Res. 1989 Dec 11;17(23):9979-91. doi: 10.1093/nar/17.23.9979.
Pubmed: 2690013
Ivanova A, Renshaw M, Guntaka RV, Eisenstark A: DNA base sequence variability in katF (putative sigma factor) gene of Escherichia coli. Nucleic Acids Res. 1992 Oct 25;20(20):5479-80. doi: 10.1093/nar/20.20.5479.
Pubmed: 1437569
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