Biochemical characterization of archaeal homocitrate synthase from Sulfolobus acidocaldarius.
Archaea
RAM domain
homocitrate synthase
lysine biosynthesis
Journal
FEBS letters
ISSN: 1873-3468
Titre abrégé: FEBS Lett
Pays: England
ID NLM: 0155157
Informations de publication
Date de publication:
01 2020
01 2020
Historique:
received:
15
05
2019
revised:
11
07
2019
accepted:
16
07
2019
pubmed:
23
7
2019
medline:
4
8
2020
entrez:
23
7
2019
Statut:
ppublish
Résumé
The hyperthermophilic archaeon, Sulfolobus, synthesizes lysine via the α-aminoadipate pathway; however, the gene encoding homocitrate synthase, the enzyme responsible for the first and committed step of the pathway, has not yet been identified. In the present study, we identified saci_1304 as the gene encoding a novel type of homocitrate synthase fused with a Regulation of Amino acid Metabolism (RAM) domain at the C terminus in Sulfolobus acidocaldarius. Enzymatic characterization revealed that Sulfolobus homocitrate synthase was inhibited by lysine; however, the mutant enzyme lacking the RAM domain was insensitive to inhibition by lysine. The present results indicated that the RAM domain is responsible for enzyme inhibition.
Identifiants
pubmed: 31330039
doi: 10.1002/1873-3468.13550
doi:
Substances chimiques
Archaeal Proteins
0
homocitrate synthase
EC 2.3.3.14
Oxo-Acid-Lyases
EC 4.1.3.-
Lysine
K3Z4F929H6
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
126-134Informations de copyright
© 2019 Federation of European Biochemical Societies.
Références
Umbarger HE (1978) Amino acid biosynthesis and its regulation. Annu Rev Biochem 47, 532-606.
Vogel HJ (1964) Distribution of lysine pathway among fungi: evolutionary implications. Am Nat 98, 446-455.
Ouchi T, Tomita T, Horie A, Yoshida A, Takahashi K, Nishida H, Lassak K, Taka H, Mineki R, Fujimura T et al. (2013) Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus. Nat Chem Biol 9, 277-283.
Kobashi N, Nishiyama M and Tanokura M (1999) Aspartate kinase-independent lysine synthesis in an extremely thermophilic bacterium, Thermus thermophilus: lysine is synthesized via α-aminoadipic acid, not via diaminopimeric acid. J Bacteriol 181, 1713-1718.
Nishida H, Nishiyama M, Kobashi N, Kosuge T, Hoshino T and Yamane H (1999) A prokaryotic gene cluster involved in synthesis of lysine through the amino adipate pathway: a key to the evolution of amino acid biosynthesis. Genome Res 9, 1175-1183.
Horie A, Tomita T, Saiki A, Kono H, Taka H, Mineki R, Fujimura T, Nishiyama C, Kuzuyama T and Nishiyama M (2009) Discovery of proteinaceous N-modification in lysine biosynthesis of Thermus thermophilus. Nat Chem Biol 5, 673-679.
Yoshida A, Tomita T, Atomi H, Kuzuyama T and Nishiyama M (2016) Lysine biosynthesis of Thermococcus kodakarensis with the capacity to function as an ornithine biosynthetic system. J Biol Chem 291, 21630-21643.
Kumar G, Johnson JL and Frantom PA (2016) Improving functional annotation in the DRE-TIM metallolyase superfamily through identification of active site fingerprints. Biochemistry 55, 1863-1872.
Yoshida A, Kosono S and Nishiyama M (2018) Characterization of two 2-isopropylmalate synthase homologs from Thermus thermophilus HB27. Biochem Biophys Res Commun 501, 465-470.
Koon N, Squire CJ and Baker EN (2004) Crystal structure of LeuA from Mycobacterium tuberculosis, a key enzyme in leucine biosynthesis. Proc Natl Acad Sci USA 101, 8295-8300.
Frantom PA (2012) Structural and functional characterization of α-isopropylmalate synthase and citramalate synthase, members of the LeuA dimer superfamily. Arch Biochem Biophys 519, 202-209.
Okada T, Tomita T, Wulandari AP, Kuzuyama T and Nishiyama M (2010) Mechanism of substrate recognition and insight into feedback inhibition of homocitrate synthase from Thermus thermophilus. J Biol Chem 285, 4195-4205.
Bulfer SL, Scott EM, Couture JF, Pillus L and Trievel RC (2009) Crystal structure and functional analysis of homocitrate synthase, an essential enzyme in lysine biosynthesis. J Biol Chem 284, 35769-35780.
Bulfer SL, Scott EM, Pillus L and Trievel RC (2010) Structural basis for L-lysine feedback inhibition of homocitrate synthase, an essential enzyme in lysine biosynthesis. J Biol Chem 285, 10446-10453.
Brinkman AB, Bell SD, Lebbink RJ, de Vos WM and van der Oost J (2002) The Sulfolobus solfataricus Lrp-like protein LysM regulates lysine biosynthesis in response to lysine availability. J Biol Chem 277, 29537-29549.
Wagner M, van Wolferen M, Wagner A, Lassak K, Meyer BH, Reimann J and Albers SV (2012) Versatile genetic tool box for the Crenarchaeote Sulfolobus acidocaldarius. Front Microbiol 3, 214.
Ellen AF, Albers SV and Driessen AJ (2010) Comparative study of the extracellular proteome of Sulfolobus species reveals limited secretion. Extremophiles 14, 87-98.
Brock TD, Brock KM, Belly RT and Weiss RL (1972) Sulfolobus: a new genus of sulfur-oxidizing bacteria living at low pH and high temperature. Arch Mikrobiol 84, 54-68.
Reindl S, Ghosh A, Williams GJ, Lassak K, Neiner T, Henche AL, Albers SV and Tainer JA (2013) Insights into FlaI functions in archaeal motor assembly and motility from structures, conformations, and genetics. Mol Cell 49, 1069-1082.
Jez JM, Ferrer JL, Bowman ME, Dixon RA and Noel JP (2000) Dissection of malonyl-coenzyme A decarboxylation from polyketide formation in the reaction mechanism of a plant polyketide synthase. Biochemistry 39, 890-902.
Hadler HI and Erwin MJ (1963) The conjugation of thiols by 2,6-dichloroindophenol. Biochemistry 2, 954-957.
Cleland WW (1979) Statistical analysis of enzyme kinetic data. Methods Enzymol 63, 103-138.
Zhang P, Ma J, Zhang Z, Zha M, Xu H, Zhao G and Ding J (2009) Molecular basis of the inhibitor selectivity and insights into the feedback inhibition mechanism of citramalate synthase from Leptospira interrogans. Biochem J 421, 133-143.
de Carvalho LP, Argyrou A and Blanchard JS (2005) Slow-onset feedback inhibition: inhibition of Mycobacterium tuberculosis α-isopropylmalate synthase by L-leucine. J Am Chem Soc 127, 10004-10005.
Ma J, Zhang P, Zhang Z, Zha M, Xu H, Zhao G and Ding J (2008) Molecular basis of the substrate specificity and the catalytic mechanism of citramalate synthase from Leptospira interrogans. Biochem J 415, 45-56.
Yokoyama K, Ishijima SA, Koike H, Kurihara C, Shimowasa A, Kabasawa M, Kawashima T and Suzuki M (2007) Feast/famine regulation by transcription factor FL11 for the survival of the hyperthermophilic archaeon Pyrococcus OT3. Structure 15, 1542-1554.
Okamura H, Yokoyama K, Koike H, Yamada M, Shimowasa A, Kabasawa M, Kawashima T and Suzuki M (2007) A structural code for discriminating between transcription signals revealed by the feast/famine regulatory protein DM1 in complex with ligands. Structure 15, 1325-1338.
Yamada M, Ishijima SA and Suzuki M (2009) Interactions between the archaeal transcription repressor FL11 and its coregulators lysine and arginine. Proteins 74, 520-525.