Logo of biochemjBJ Latest papers and much more!
Biochem J. 1999 Dec 15; 344(Pt 3): 633–642.
PMCID: PMC1220684

Polyamine transport in bacteria and yeast.


The polyamine content of cells is regulated by biosynthesis, degradation and transport. In Escherichia coli, the genes for three different polyamine transport systems have been cloned and characterized. Two uptake systems (putrescine-specific and spermidine-preferential) were ABC transporters, each consisting of a periplasmic substrate-binding protein, two transmembrane proteins and a membrane-associated ATPase. The crystal structures of the substrate-binding proteins (PotD and PotF) have been solved. They consist of two domains with an alternating beta-alpha-beta topology, similar to other periplasmic binding proteins. The polyamine-binding site is in a cleft between the two domains, as determined by crystallography and site-directed mutagenesis. Polyamines are mainly recognized by aspartic acid and glutamic acid residues, which interact with the NH(2)- (or NH-) groups, and by tryptophan and tyrosine residues that have hydrophobic interactions with the methylene groups of polyamines. The precursor of one of the substrate binding proteins, PotD, negatively regulates transcription of the operon for the spermidine-preferential uptake system, thus providing another level of regulation of cellular polyamines. The third transport system, catalysed by PotE, mediates both uptake and excretion of putrescine. Uptake of putrescine is dependent on membrane potential, whereas excretion involves an exchange reaction between putrescine and ornithine. In Saccharomyces cerevisiae, the gene for a polyamine transport protein (TPO1) was identified. The properties of this protein are similar to those of PotE, and TPO1 is located on the vacuolar membrane.

Full Text

The Full Text of this article is available as a PDF (419K).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Tabor CW, Tabor H. Polyamines. Annu Rev Biochem. 1984;53:749–790. [PubMed]
  • Pegg AE. Polyamine metabolism and its importance in neoplastic growth and a target for chemotherapy. Cancer Res. 1988 Feb 15;48(4):759–774. [PubMed]
  • Kano K, Oka T. Polyamine transport and metabolism in mouse mammary gland. General properties and hormonal regulation. J Biol Chem. 1976 May 10;251(9):2795–2800. [PubMed]
  • Pohjanpelto P. Putrescine transport is greatly increased in human fibroblasts initiated to proliferate. J Cell Biol. 1976 Mar;68(3):512–520. [PMC free article] [PubMed]
  • Porter CW, Miller J, Bergeron RJ. Aliphatic chain length specificity of the polyamine transport system in ascites L1210 leukemia cells. Cancer Res. 1984 Jan;44(1):126–128. [PubMed]
  • Kakinuma Y, Hoshino K, Igarashi K. Characterization of the inducible polyamine transporter in bovine lymphocytes. Eur J Biochem. 1988 Sep 15;176(2):409–414. [PubMed]
  • Byers TL, Kameji R, Rannels DE, Pegg AE. Multiple pathways for uptake of paraquat, methylglyoxal bis(guanylhydrazone), and polyamines. Am J Physiol. 1987 Jun;252(6 Pt 1):C663–C669. [PubMed]
  • Kashiwagi K, Kobayashi H, Igarashi K. Apparently unidirectional polyamine transport by proton motive force in polyamine-deficient Escherichia coli. J Bacteriol. 1986 Mar;165(3):972–977. [PMC free article] [PubMed]
  • Munro GF, Bell CA, Lederman M. Multiple transport components for putrescine in Escherichia coli. J Bacteriol. 1974 Jun;118(3):952–963. [PMC free article] [PubMed]
  • Kashiwagi K, Hosokawa N, Furuchi T, Kobayashi H, Sasakawa C, Yoshikawa M, Igarashi K. Isolation of polyamine transport-deficient mutants of Escherichia coli and cloning of the genes for polyamine transport proteins. J Biol Chem. 1990 Dec 5;265(34):20893–20897. [PubMed]
  • Tomitori H, Kashiwagi K, Sakata K, Kakinuma Y, Igarashi K. Identification of a gene for a polyamine transport protein in yeast. J Biol Chem. 1999 Feb 5;274(6):3265–3267. [PubMed]
  • Igarashi K, Kashiwagi K, Hamasaki H, Miura A, Kakegawa T, Hirose S, Matsuzaki S. Formation of a compensatory polyamine by Escherichia coli polyamine-requiring mutants during growth in the absence of polyamines. J Bacteriol. 1986 Apr;166(1):128–134. [PMC free article] [PubMed]
  • Hyde SC, Emsley P, Hartshorn MJ, Mimmack MM, Gileadi U, Pearce SR, Gallagher MP, Gill DR, Hubbard RE, Higgins CF. Structural model of ATP-binding proteins associated with cystic fibrosis, multidrug resistance and bacterial transport. Nature. 1990 Jul 26;346(6282):362–365. [PubMed]
  • Furuchi T, Kashiwagi K, Kobayashi H, Igarashi K. Characteristics of the gene for a spermidine and putrescine transport system that maps at 15 min on the Escherichia coli chromosome. J Biol Chem. 1991 Nov 5;266(31):20928–20933. [PubMed]
  • Pistocchi R, Kashiwagi K, Miyamoto S, Nukui E, Sadakata Y, Kobayashi H, Igarashi K. Characteristics of the operon for a putrescine transport system that maps at 19 minutes on the Escherichia coli chromosome. J Biol Chem. 1993 Jan 5;268(1):146–152. [PubMed]
  • Walker JE, Saraste M, Runswick MJ, Gay NJ. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1982;1(8):945–951. [PMC free article] [PubMed]
  • Ames GF. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu Rev Biochem. 1986;55:397–425. [PubMed]
  • Kashiwagi K, Endo H, Kobayashi H, Takio K, Igarashi K. Spermidine-preferential uptake system in Escherichia coli. ATP hydrolysis by PotA protein and its association with membrane. J Biol Chem. 1995 Oct 27;270(43):25377–25382. [PubMed]
  • Kashiwagi K, Miyamoto S, Nukui E, Kobayashi H, Igarashi K. Functions of potA and potD proteins in spermidine-preferential uptake system in Escherichia coli. J Biol Chem. 1993 Sep 15;268(26):19358–19363. [PubMed]
  • Hung LW, Wang IX, Nikaido K, Liu PQ, Ames GF, Kim SH. Crystal structure of the ATP-binding subunit of an ABC transporter. Nature. 1998 Dec 17;396(6712):703–707. [PubMed]
  • Sugiyama S, Vassylyev DG, Matsushima M, Kashiwagi K, Igarashi K, Morikawa K. Crystal structure of PotD, the primary receptor of the polyamine transport system in Escherichia coli. J Biol Chem. 1996 Apr 19;271(16):9519–9525. [PubMed]
  • Sugiyama S, Matsuo Y, Maenaka K, Vassylyev DG, Matsushima M, Kashiwagi K, Igarashi K, Morikawa K. The 1.8-A X-ray structure of the Escherichia coli PotD protein complexed with spermidine and the mechanism of polyamine binding. Protein Sci. 1996 Oct;5(10):1984–1990. [PMC free article] [PubMed]
  • Kashiwagi K, Pistocchi R, Shibuya S, Sugiyama S, Morikawa K, Igarashi K. Spermidine-preferential uptake system in Escherichia coli. Identification of amino acids involved in polyamine binding in PotD protein. J Biol Chem. 1996 May 24;271(21):12205–12208. [PubMed]
  • Kang CH, Shin WC, Yamagata Y, Gokcen S, Ames GF, Kim SH. Crystal structure of the lysine-, arginine-, ornithine-binding protein (LAO) from Salmonella typhimurium at 2.7-A resolution. J Biol Chem. 1991 Dec 15;266(35):23893–23899. [PubMed]
  • Oh BH, Pandit J, Kang CH, Nikaido K, Gokcen S, Ames GF, Kim SH. Three-dimensional structures of the periplasmic lysine/arginine/ornithine-binding protein with and without a ligand. J Biol Chem. 1993 May 25;268(15):11348–11355. [PubMed]
  • Sack JS, Saper MA, Quiocho FA. Periplasmic binding protein structure and function. Refined X-ray structures of the leucine/isoleucine/valine-binding protein and its complex with leucine. J Mol Biol. 1989 Mar 5;206(1):171–191. [PubMed]
  • Sack JS, Trakhanov SD, Tsigannik IH, Quiocho FA. Structure of the L-leucine-binding protein refined at 2.4 A resolution and comparison with the Leu/Ile/Val-binding protein structure. J Mol Biol. 1989 Mar 5;206(1):193–207. [PubMed]
  • Sun YJ, Rose J, Wang BC, Hsiao CD. The structure of glutamine-binding protein complexed with glutamine at 1.94 A resolution: comparisons with other amino acid binding proteins. J Mol Biol. 1998 Apr 24;278(1):219–229. [PubMed]
  • Nickitenko AV, Trakhanov S, Quiocho FA. 2 A resolution structure of DppA, a periplasmic dipeptide transport/chemosensory receptor. Biochemistry. 1995 Dec 26;34(51):16585–16595. [PubMed]
  • Tame JR, Murshudov GN, Dodson EJ, Neil TK, Dodson GG, Higgins CF, Wilkinson AJ. The structural basis of sequence-independent peptide binding by OppA protein. Science. 1994 Jun 10;264(5165):1578–1581. [PubMed]
  • Pflugrath JW, Quiocho FA. The 2 A resolution structure of the sulfate-binding protein involved in active transport in Salmonella typhimurium. J Mol Biol. 1988 Mar 5;200(1):163–180. [PubMed]
  • Luecke H, Quiocho FA. High specificity of a phosphate transport protein determined by hydrogen bonds. Nature. 1990 Sep 27;347(6291):402–406. [PubMed]
  • Quiocho FA, Vyas NK. Novel stereospecificity of the L-arabinose-binding protein. Nature. 1984 Aug 2;310(5976):381–386. [PubMed]
  • Vyas NK, Vyas MN, Quiocho FA. Sugar and signal-transducer binding sites of the Escherichia coli galactose chemoreceptor protein. Science. 1988 Dec 2;242(4883):1290–1295. [PubMed]
  • Mowbray SL, Cole LB. 1.7 A X-ray structure of the periplasmic ribose receptor from Escherichia coli. J Mol Biol. 1992 May 5;225(1):155–175. [PubMed]
  • Sharff AJ, Rodseth LE, Spurlino JC, Quiocho FA. Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis. Biochemistry. 1992 Nov 10;31(44):10657–10663. [PubMed]
  • Spurlino JC, Lu GY, Quiocho FA. The 2.3-A resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis. J Biol Chem. 1991 Mar 15;266(8):5202–5219. [PubMed]
  • Chaudhuri BN, Ko J, Park C, Jones TA, Mowbray SL. Structure of D-allose binding protein from Escherichia coli bound to D-allose at 1.8 A resolution. J Mol Biol. 1999 Mar 12;286(5):1519–1531. [PubMed]
  • Vassylyev DG, Tomitori H, Kashiwagi K, Morikawa K, Igarashi K. Crystal structure and mutational analysis of the Escherichia coli putrescine receptor. Structural basis for substrate specificity. J Biol Chem. 1998 Jul 10;273(28):17604–17609. [PubMed]
  • Fleischmann RD, Adams MD, White O, Clayton RA, Kirkness EF, Kerlavage AR, Bult CJ, Tomb JF, Dougherty BA, Merrick JM, et al. Whole-genome random sequencing and assembly of Haemophilus influenzae Rd. Science. 1995 Jul 28;269(5223):496–512. [PubMed]
  • Kulakova AN, Kulakov LA, Quinn JP. Cloning of the phosphonoacetate hydrolase gene from Pseudomonas fluorescens 23F encoding a new type of carbon-phosphorus bond cleaving enzyme and its expression in Escherichia coli and Pseudomonas putida. Gene. 1997 Aug 11;195(1):49–53. [PubMed]
  • Fraser CM, Casjens S, Huang WM, Sutton GG, Clayton R, Lathigra R, White O, Ketchum KA, Dodson R, Hickey EK, et al. Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi. Nature. 1997 Dec 11;390(6660):580–586. [PubMed]
  • Fraser CM, Norris SJ, Weinstock GM, White O, Sutton GG, Dodson R, Gwinn M, Hickey EK, Clayton R, Ketchum KA, et al. Complete genome sequence of Treponema pallidum, the syphilis spirochete. Science. 1998 Jul 17;281(5375):375–388. [PubMed]
  • Kashiwagi K, Suzuki T, Suzuki F, Furuchi T, Kobayashi H, Igarashi K. Coexistence of the genes for putrescine transport protein and ornithine decarboxylase at 16 min on Escherichia coli chromosome. J Biol Chem. 1991 Nov 5;266(31):20922–20927. [PubMed]
  • Kashiwagi K, Shibuya S, Tomitori H, Kuraishi A, Igarashi K. Excretion and uptake of putrescine by the PotE protein in Escherichia coli. J Biol Chem. 1997 Mar 7;272(10):6318–6323. [PubMed]
  • Kashiwagi K, Miyamoto S, Suzuki F, Kobayashi H, Igarashi K. Excretion of putrescine by the putrescine-ornithine antiporter encoded by the potE gene of Escherichia coli. Proc Natl Acad Sci U S A. 1992 May 15;89(10):4529–4533. [PMC free article] [PubMed]
  • Tatusov RL, Mushegian AR, Bork P, Brown NP, Hayes WS, Borodovsky M, Rudd KE, Koonin EV. Metabolism and evolution of Haemophilus influenzae deduced from a whole-genome comparison with Escherichia coli. Curr Biol. 1996 Mar 1;6(3):279–291. [PubMed]
  • Kaback HR. Use of site-directed mutagenesis to study the mechanism of a membrane transport protein. Biochemistry. 1987 Apr 21;26(8):2071–2076. [PubMed]
  • Poolman B, Modderman R, Reizer J. Lactose transport system of Streptococcus thermophilus. The role of histidine residues. J Biol Chem. 1992 May 5;267(13):9150–9157. [PubMed]
  • Yamaguchi A, Nakatani M, Sawai T. Aspartic acid-66 is the only essential negatively charged residue in the putative hydrophilic loop region of the metal-tetracycline/H+ antiporter encoded by transposon Tn10 of Escherichia coli. Biochemistry. 1992 Sep 8;31(35):8344–8348. [PubMed]
  • Meng SY, Bennett GN. Nucleotide sequence of the Escherichia coli cad operon: a system for neutralization of low extracellular pH. J Bacteriol. 1992 Apr;174(8):2659–2669. [PMC free article] [PubMed]
  • Blattner FR, Plunkett G, 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, et al. The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453–1462. [PubMed]
  • Molenaar D, Bosscher JS, ten Brink B, Driessen AJ, Konings WN. Generation of a proton motive force by histidine decarboxylation and electrogenic histidine/histamine antiport in Lactobacillus buchneri. J Bacteriol. 1993 May;175(10):2864–2870. [PMC free article] [PubMed]
  • Oshima T, Hamasaki N, Senshu M, Kakinuma K, Kuwajima I. A new naturally occurring polyamine containing a quaternary ammonium nitrogen. J Biol Chem. 1987 Sep 5;262(25):11979–11981. [PubMed]
  • Fraser CM, Gocayne JD, White O, Adams MD, Clayton RA, Fleischmann RD, Bult CJ, Kerlavage AR, Sutton G, Kelley JM, et al. The minimal gene complement of Mycoplasma genitalium. Science. 1995 Oct 20;270(5235):397–403. [PubMed]
  • Antognoni F, Del Duca S, Kuraishi A, Kawabe E, Fukuchi-Shimogori T, Kashiwagi K, Igarashi K. Transcriptional inhibition of the operon for the spermidine uptake system by the substrate-binding protein PotD. J Biol Chem. 1999 Jan 22;274(4):1942–1948. [PubMed]
  • Jishage M, Ishihama A. Regulation of RNA polymerase sigma subunit synthesis in Escherichia coli: intracellular levels of sigma 70 and sigma 38. J Bacteriol. 1995 Dec;177(23):6832–6835. [PMC free article] [PubMed]
  • Nomura M, Gourse R, Baughman G. Regulation of the synthesis of ribosomes and ribosomal components. Annu Rev Biochem. 1984;53:75–117. [PubMed]
  • Muro-Pastor AM, Maloy S. Proline dehydrogenase activity of the transcriptional repressor PutA is required for induction of the put operon by proline. J Biol Chem. 1995 Apr 28;270(17):9819–9827. [PubMed]
  • Kashiwagi K, Watanabe R, Igarashi K. Involvement of ribonuclease III in the enhancement of expression of the speF-potE operon encoding inducible ornithine decarboxylase and polyamine transport protein. Biochem Biophys Res Commun. 1994 Apr 15;200(1):591–597. [PubMed]
  • Kameyama L, Fernandez L, Court DL, Guarneros G. RNaselll activation of bacteriophage lambda N synthesis. Mol Microbiol. 1991 Dec;5(12):2953–2963. [PubMed]
  • Dunn JJ, Studier FW. Effect of RNAase III, cleavage on translation of bacteriophage T7 messenger RNAs. J Mol Biol. 1975 Dec 15;99(3):487–499. [PubMed]
  • Maruyama T, Masuda N, Kakinuma Y, Igarashi K. Polyamine-sensitive magnesium transport in Saccharomyces cerevisiae. Biochim Biophys Acta. 1994 Sep 14;1194(2):289–295. [PubMed]
  • Kakinuma Y, Maruyama T, Nozaki T, Wada Y, Ohsumi Y, Igarashi K. Cloning of the gene encoding a putative serine/threonine protein kinase which enhances spermine uptake in Saccharomyces cerevisiae. Biochem Biophys Res Commun. 1995 Nov 22;216(3):985–992. [PubMed]
  • Nozaki T, Nishimura K, Michael AJ, Maruyama T, Kakinuma Y, Igarashi K. A second gene encoding a putative serine/threonine protein kinase which enhances spermine uptake in Saccharomyces cerevisiae. Biochem Biophys Res Commun. 1996 Nov 12;228(2):452–458. [PubMed]
  • Kaouass M, Audette M, Ramotar D, Verma S, De Montigny D, Gamache I, Torossian K, Poulin R. The STK2 gene, which encodes a putative Ser/Thr protein kinase, is required for high-affinity spermidine transport in Saccharomyces cerevisiae. Mol Cell Biol. 1997 Jun;17(6):2994–3004. [PMC free article] [PubMed]
  • Kaouass M, Gamache I, Ramotar D, Audette M, Poulin R. The spermidine transport system is regulated by ligand inactivation, endocytosis, and by the Npr1p Ser/Thr protein kinase in Saccharomyces cerevisiae. J Biol Chem. 1998 Jan 23;273(4):2109–2117. [PubMed]
  • Woolridge DP, Vazquez-Laslop N, Markham PN, Chevalier MS, Gerner EW, Neyfakh AA. Efflux of the natural polyamine spermidine facilitated by the Bacillus subtilis multidrug transporter Blt. J Biol Chem. 1997 Apr 4;272(14):8864–8866. [PubMed]
  • Goffeau A, Barrell BG, Bussey H, Davis RW, Dujon B, Feldmann H, Galibert F, Hoheisel JD, Jacq C, Johnston M, et al. Life with 6000 genes. Science. 1996 Oct 25;274(5287):546–567. [PubMed]
  • Kakinuma Y, Masuda N, Igarashi K. Proton potential-dependent polyamine transport by vacuolar membrane vesicles of Saccharomyces cerevisiae. Biochim Biophys Acta. 1992 Jun 11;1107(1):126–130. [PubMed]
  • Williams K, Kashiwagi K, Fukuchi J, Igarashi K. An acidic amino acid in the N-methyl-D-aspartate receptor that is important for spermine stimulation. Mol Pharmacol. 1995 Dec;48(6):1087–1098. [PubMed]
  • Kashiwagi K, Fukuchi J, Chao J, Igarashi K, Williams K. An aspartate residue in the extracellular loop of the N-methyl-D-aspartate receptor controls sensitivity to spermine and protons. Mol Pharmacol. 1996 Jun;49(6):1131–1141. [PubMed]
  • Chao J, Seiler N, Renault J, Kashiwagi K, Masuko T, Igarashi K, Williams K. N1-dansyl-spermine and N1-(n-octanesulfonyl)-spermine, novel glutamate receptor antagonists: block and permeation of N-methyl-D-aspartate receptors. Mol Pharmacol. 1997 May;51(5):861–871. [PubMed]
  • Masuko T, Kashiwagi K, Kuno T, Nguyen ND, Pahk AJ, Fukuchi J, Igarashi K, Williams K. A regulatory domain (R1-R2) in the amino terminus of the N-methyl-D-aspartate receptor: effects of spermine, protons, and ifenprodil, and structural similarity to bacterial leucine/isoleucine/valine binding protein. Mol Pharmacol. 1999 Jun;55(6):957–969. [PubMed]
  • Mitchell JL, Diveley RR, Jr, Bareyal-Leyser A, Mitchell JL. Abnormal accumulation and toxicity of polyamines in a difluoromethylornithine-resistant HTC cell variant. Biochim Biophys Acta. 1992 Aug 12;1136(2):136–142. [PubMed]
  • Suzuki T, He Y, Kashiwagi K, Murakami Y, Hayashi S, Igarashi K. Antizyme protects against abnormal accumulation and toxicity of polyamines in ornithine decarboxylase-overproducing cells. Proc Natl Acad Sci U S A. 1994 Sep 13;91(19):8930–8934. [PMC free article] [PubMed]
  • Mitchell JL, Judd GG, Bareyal-Leyser A, Ling SY. Feedback repression of polyamine transport is mediated by antizyme in mammalian tissue-culture cells. Biochem J. 1994 Apr 1;299(Pt 1):19–22. [PMC free article] [PubMed]
  • He Y, Suzuki T, Kashiwagi K, Igarashi K. Antizyme delays the restoration by spermine of growth of polyamine-deficient cells through its negative regulation of polyamine transport. Biochem Biophys Res Commun. 1994 Aug 30;203(1):608–614. [PubMed]
  • Sakata K, Fukuchi-Shimogori T, Kashiwagi K, Igarashi K. Identification of regulatory region of antizyme necessary for the negative regulation of polyamine transport. Biochem Biophys Res Commun. 1997 Sep 18;238(2):415–419. [PubMed]
  • Tabor CW, Tabor H. The speEspeD operon of Escherichia coli. Formation and processing of a proenzyme form of S-adenosylmethionine decarboxylase. J Biol Chem. 1987 Nov 25;262(33):16037–16040. [PubMed]
  • Fukuchi J, Kashiwagi K, Takio K, Igarashi K. Properties and structure of spermidine acetyltransferase in Escherichia coli. J Biol Chem. 1994 Sep 9;269(36):22581–22585. [PubMed]
  • Moore RC, Boyle SM. Nucleotide sequence and analysis of the speA gene encoding biosynthetic arginine decarboxylase in Escherichia coli. J Bacteriol. 1990 Aug;172(8):4631–4640. [PMC free article] [PubMed]
  • Boyle SM, Barroso L, Moore RC, Wright JM, Patel T. Primary structure of the speC gene encoding biosynthetic ornithine decarboxylase in Escherichia coli. Gene. 1994 Dec 30;151(1-2):157–160. [PubMed]
  • Bollinger JM, Jr, Kwon DS, Huisman GW, Kolter R, Walsh CT. Glutathionylspermidine metabolism in Escherichia coli. Purification, cloning, overproduction, and characterization of a bifunctional glutathionylspermidine synthetase/amidase. J Biol Chem. 1995 Jun 9;270(23):14031–14041. [PubMed]
  • Stim KP, Bennett GN. Nucleotide sequence of the adi gene, which encodes the biodegradative acid-induced arginine decarboxylase of Escherichia coli. J Bacteriol. 1993 Mar;175(5):1221–1234. [PMC free article] [PubMed]
  • Stim-Herndon KP, Flores TM, Bennett GN. Molecular characterization of adiY, a regulatory gene which affects expression of the biodegradative acid-induced arginine decarboxylase gene (adiA) of Escherichia coli. Microbiology. 1996 May;142(Pt 5):1311–1320. [PubMed]
  • Watson N, Dunyak DS, Rosey EL, Slonczewski JL, Olson ER. Identification of elements involved in transcriptional regulation of the Escherichia coli cad operon by external pH. J Bacteriol. 1992 Jan;174(2):530–540. [PMC free article] [PubMed]
  • Ota M, Nishikawa K. Assessment of pseudo-energy potentials by the best-five test: a new use of the three-dimensional profiles of proteins. Protein Eng. 1997 Apr;10(4):339–351. [PubMed]
  • Klenk HP, Clayton RA, Tomb JF, White O, Nelson KE, Ketchum KA, Dodson RJ, Gwinn M, Hickey EK, Peterson JD, et al. The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus. Nature. 1997 Nov 27;390(6658):364–370. [PubMed]
  • Himmelreich R, Hilbert H, Plagens H, Pirkl E, Li BC, Herrmann R. Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae. Nucleic Acids Res. 1996 Nov 15;24(22):4420–4449. [PMC free article] [PubMed]
  • Andersson SG, Zomorodipour A, Andersson JO, Sicheritz-Pontén T, Alsmark UC, Podowski RM, Näslund AK, Eriksson AS, Winkler HH, Kurland CG. The genome sequence of Rickettsia prowazekii and the origin of mitochondria. Nature. 1998 Nov 12;396(6707):133–140. [PubMed]
  • Kaneko T, Sato S, Kotani H, Tanaka A, Asamizu E, Nakamura Y, Miyajima N, Hirosawa M, Sugiura M, Sasamoto S, et al. Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. DNA Res. 1996 Jun 30;3(3):109–136. [PubMed]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society


Related citations in PubMed

See reviews...See all...

Cited by other articles in PMC

See all...


Recent Activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...