The eutt enzyme of salmonella enterica is a unique atp: Cob(i)alamin adenosyltransferase metalloprotein that requires ferrous ions for maximal activity

Journal of Bacteriology

Volumn 196, Issue 4, 2014, Pages 903-910

  Moore, Theodore C ^a   Mera, Paola E ^b,c   Escalante Semerena, Jorge C ^a  

^a UNIVERSITY OF GEORGIA   (United States)

^b UNIVERSITY OF WISCONSIN MADISON   (United States)

^c STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BACTERIAL ENZYME; CHOLESTEROL ACYLTRANSFERASE; EUTT ENZYME; FERROUS ION; HYDROGEN PEROXIDE; METALLOPROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CHEMICAL REACTION KINETICS; CIRCULAR DICHROISM; ENZYME ACTIVITY; ENZYME PURIFICATION; IN VITRO STUDY; IN VIVO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN INTERACTION; SALMONELLA ENTERICA;

ADENOSINE TRIPHOSPHATE; ALKYL AND ARYL TRANSFERASES; CHROMATOGRAPHY, LIQUID; COENZYMES; DNA MUTATIONAL ANALYSIS; FERROUS COMPOUNDS; IONS; KINETICS; METALLOPROTEINS; PROTEIN MULTIMERIZATION; SALMONELLA ENTERICA;

EID: 84893018704     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01304-13     Document Type: Article

References (37)

1. Mera PE, Escalante-Semerena JC. 2010. Multiple roles of ATP: cob(I)alamin adenosyltransferases in the conversion of B(12) to coenzyme B (12). Appl. Microbiol. Biotechnol. 88:41-48. http://dx.doi.org/10 .1007/s00253-010-2773-2.
2. Escalante-Semerena JC, Suh SJ, Roth JR. 1990. cobA function is required for both de novo cobalamin biosynthesis and assimilation of exogenous corrinoids in Salmonella typhimurium. J. Bacteriol. 172:273-280.
3. Suh S, Escalante-Semerena JC. 1995. Purification and initial characterization of the ATP:corrinoid adenosyltransferase encoded by the cobA gene of Salmonella typhimurium. J. Bacteriol. 177:921-925.
4. Mera PE, Maurice MS, Rayment I, Escalante-Semerena JC. 2007. Structural and functional analyses of the human-type corrinoid adenosyltransferase (PduO) from Lactobacillus reuteri. Biochemistry 46:13829-13836. http://dx.doi.org/10.1021/bi701622j.
5. Mera PE, St Maurice M, Rayment I, Escalante-Semerena JC. 2009. Residue Phe112 of the human-type corrinoid adenosyltransferase (PduO) enzyme of Lactobacillus reuteri is critical to the formation of the fourcoordinate Co(II) corrinoid substrate and to the activity of the enzyme. Biochemistry 48:3138-3145. http://dx.doi.org/10.1021/bi9000134
6. Buan NR, Escalante-Semerena JC. 2006. Purification and initial biochemical characterization of ATP:cob(I)alamin adenosyltransferase (EutT) enzyme of Salmonella enterica. J. Biol. Chem. 281:16971-16977. http://dx.doi.org/10.1074/jbc.M603069200
7. Buan NR, Suh SJ, Escalante-Semerena JC. 2004. The eutT gene of Salmonella enterica encodes an oxygen-labile, metal-containing ATP: corrinoid adenosyltransferase enzyme. J. Bacteriol. 186:5708-5714. http: //dx.doi.org/10.1128/JB.186.17.5708-5714.2004
8. Johnson CL, Buszko ML, Bobik TA. 2004. Purification and initial characterization of the Salmonella enterica PduO ATP:Cob(I)alamin adenosyltransferase. J. Bacteriol. 186:7881-7887. http://dx.doi.org/10.1128/JB.186 .23.7881-7887.2004
9. Johnson CL, Pechonick E, Park SD, Havemann GD, Leal NA, Bobik TA. 2001. Functional genomic, biochemical, and genetic characterization of the Salmonella pduO gene, an ATP:cob(I)alamin adenosyltransferase gene. J. Bacteriol. 183:1577-1584. http://dx.doi.org/10.1128/JB.183.5 .1577-1584.2001
10. Stich TA, Yamanishi M, Banerjee R, Brunold TC. 2005. Spectroscopic evidence for the formation of a four-coordinate Co(2+)cobalamin species upon binding to the human ATP:cobalamin adenosyltransferase. J. Am. Chem. Soc. 127:7660-7661. http://dx.doi.org/10.1021/ja050546r
11. Stich TA, Buan NR, Escalante-Semerena JC, Brunold TC. 2005. Spectroscopic and computational studies of the ATP:corrinoid adenosyltransferase (CobA) from Salmonella enterica: insights into the mechanism of adenosylcobalamin biosynthesis. J. Am. Chem. Soc. 127:8710-8719. http: //dx.doi.org/10.1021/ja042142p
12. Park K, Mera PE, Escalante-Semerena JC, Brunold TC. 2008. Kinetic and spectroscopic studies of the ATP:corrinoid adenosyltransferase PduO from Lactobacillus reuteri: substrate specificity and insights into the mechanism of Co(II)corrinoid reduction. Biochemistry 47:9007-9015. http: //dx.doi.org/10.1021/bi800419e
13. Moore TC, Newmister SA, Rayment I, Escalante-Semerena JC. 2012. Structural insights into the mechanism of four-coordinate cob(II)alamin formation in the active site of the Salmonella enterica ATP:co(I)rrinoid adenosyltransferase (CobA) enzyme: critical role of residues Phe91 and Trp93. Biochemistry 51:9647-9657. http://dx.doi.org/10.1021/bi301378d
14. Rocco CJ, Dennison KL, Klenchin VA, Rayment I, Escalante-Semerena JC. 2008. Construction and use of new cloning vectors for the rapid isolation of recombinant proteins from Escherichia coli. Plasmid 59:231-237. http://dx.doi.org/10.1016/j.plasmid.2008.01.001
15. Blommel PG, Fox BG. 2007. A combined approach to improving largescale production of tobacco etch virus protease. Protein Expr. Purif. 55: 53-68. http://dx.doi.org/10.1016/j.pep.2007.04.013
16. Gasteiger E, Gattiker A, Hoogland C, Ivanyi I, Appel RD, Bairoch A. 2003. ExPASy: the proteomics server for in-depth protein knowledge and analysis. Nucleic Acids Res. 31:3784-3788. http://dx.doi.org/10.1093/nar /gkg563
17. St Maurice M, Mera PE, Taranto MP, Sesma F, Escalante-Semerena JC, Rayment I. 2007. Structural characterization of the active site of the PduOtype ATP:Co(I)rrinoid adenosyltransferase from Lactobacillus reuteri. J. Biol. Chem. 282:2596-2605. http://dx.doi.org/10.1074/jbc.M609557200
18. Hogenkamp HPC, Pailes WH, Brownson C. 1971. Preparation of 5=- deoxyadenosylcobalamin and analogs containing modified nucleosides, p 57-71. In McCormick DB, Wright LD (ed), Vitamins and coenzymes, vol 18C. Academic Press, Inc., New York, NY
19. Zehnder AJ, Wuhrmann K. 1976. Titanium (III) citrate as a nontoxic oxidation-reduction buffering system for the culture of obligate anaerobes. Science 194:1165-1166. http://dx.doi.org/10.1126/science.793008
20. Mera PE, Escalante-Semerena JC. 2010. Dihydroflavin-driven adenosylation of 4-coordinate Co(II) corrinoids: are cobalamin reductases enzymes or electron transfer proteins? J. Biol. Chem. 285:2911-2917. http: //dx.doi.org/10.1074/jbc.M109.059485
21. Vogel HJ, Bonner DM. 1956. Acetylornithinase of Escherichia coli: partial purification and some properties. J. Biol. Chem. 218:97-106
22. Berkowitz D, Hushon JM, Whitfield HJ, Jr, Roth J, Ames BN. 1968. Procedure for identifying nonsense mutations. J. Bacteriol. 96:215-220
23. Balch WE, Wolfe RS. 1976. New approach to the cultivation of methanogenic bacteria: 2-mercaptoethanesulfonic acid (HS-CoM)-dependent growth of Methanobacterium ruminantium in a pressurized atmosphere. Appl. Environ. Microbiol. 32:781-791
24. Guzman LM, Belin D, Carson MJ, Beckwith J. 1995. Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol. 177:4121-4130
25. Wilson AC, Pardee AB. 1962. Regulation of flavin synthesis by Escherichia coli. J. Gen. Microbiol. 28:283-303. http://dx.doi.org/10.1099/00221287 -28-2-283
26. Brindley AA, Raux E, Leech HK, Schubert HL, Warren MJ. 2003. A story of chelatase evolution: identification and characterization of a small 13-15-kDa "ancestral" cobaltochelatase (CbiXS) in the archaea. J. Biol. Chem. 278:22388-22395. http://dx.doi.org/10.1074/jbc.M302468200
27. Tetlow JA, Wilson AL. 1964. The absorptiometric determination of iron in boiler feed-water. Part III. Method for determining the total iron content. Analyst 89:442-452
28. Torrance JD, Bothwell TH. 1968. A simple technique for measuring storage iron concentrations in formalinised liver samples. South Afric. J. Med. Sci. 33:9-11
29. Sobota JM, Imlay JA. 2011. Iron enzyme ribulose-5-phosphate 3-epimerase in Escherichia coli is rapidly damaged by hydrogen peroxide but can be protected by manganese. Proc. Natl. Acad. Sci. U. S. A. 108:5402-5407. http://dx.doi.org/10.1073/pnas.1100410108
30. Rouf MA. 1964. Spectrochemical analysis of inorganic elements in bacteria. J. Bacteriol. 88:1545-1549
31. 2, Fe2+, and Mn2+. J. Bacteriol. 184:3151-3158. http://dx.doi.org/10 .1128/JB.184.12.3151-3158.2002
32. Rowe JL, Starnes GL, Chivers PT. 2005. Complex transcriptional control links NikABCDE-dependent nickel transport with hydrogenase expression in Escherichia coli. J. Bacteriol. 187:6317-6323. http://dx.doi.org/10 .1128/JB.187.18.6317-6323.2005
33. Gagnon P. 2006. Practical strategies for protein contaminant detection by high performance ion exchange chromatography, p. 67-79. In Rodribuez-Diaz R, Wehr T, Tuck S (ed), Analytical techniques for biopharmaceutical development. Marcel Dekker, New York, NY
34. Kay A. 2004. Detecting and minimizing zinc contamination in physiological solutions. BMC Physiol. 4:4. http://dx.doi.org/10.1186/1472 -6793-4-4
35. Fonseca MV, Escalante-Semerena JC. 2001. An in vitro reducing system for the enzymic conversion of cobalamin to adenosylcobalamin. J. Biol. Chem. 276:32101-32108. http://dx.doi.org/10.1074/jbc .M102510200
36. Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.) 227:680-685. http://dx.doi .org/10.1038/227680a0
37. Sasse J. 1991. Detection of proteins, p 10.16.11-10.16.18. In Ausubel FA, Brent R, Kingston RE, Moore DD, Seidman JG, Smith JA, Struhl K (ed), Current protocols in molecular biology, vol 1. Wiley Interscience, New York, NY