Abstract
Antisera were prepared against homogeneous serine hydroxymethyltransferase (SHMT) of an obligate methylotroph, Hyphomicrobium methylovorum GM2. Cell-free extracts of methylotrophic and non-methylotrophic microorganisms, rat and rabbit liver, which showed SHMT activities, were tested for immunological corss-reactivity with the anti-H. methylovorum GM2-SHMT. The extracts of only six methylotrophic strains showed reactivities These bacterial strains were all found to belong to the genus Hyphomicrobium on the basis of electron microscopy and C1-compound utilization. The cross-reaction test using the anti-H. methylovorum GM2-SHMT was also applied to various Hyphomicrobium strains. With the exception of H. neptunium, which has previously been recommended to be transferred to another genus, cell-free extracts of all the strains formed precipitin lines; some of them fused and the other spurred with each other. Thus, it was concluded that SHMT enzymes of methylotrophic Hyphomicrobium strains are immunologically related closely to each other and that the SHMT of H. methylovorum is an antigen specific for the genus Hyphomicrobium.
Similar content being viewed by others
Abbreviations
- SHMT:
-
serine hydroxymethyltransferase
- C1 :
-
onecarbon
References
Anthony C (1982) The serine pathway of formaldehyde assimilation. In: Buchanan RE (ed) The biochemistry of methylotroph. Academic Press, New York, pp 95–132
Bergey's Manual (1974) Bergey's manual of determinative bacteriology, 8th edn. Waverly, pp 148–153
Bradford M (1976) A rapid and sensitive method for the quantification of microgram quantities of protein using the principle of protein dye binding. Anal Biochem 72:248–254
Fujioka M (1969) Purification and properties of serine hydroxymethyltransferase from soluble and mitochondrial fractions of rabbit livers. Biochim Biophys Acta 185:338–349
Gasser F, Gasser C (1971) Immunological relationships among lactic dehydrogenases in the genera Lactobacillus and Leuconostoc. J Bacteriol 106:113–125
Ghisalba O, Kuenzi, M (1893) Biodegradation and utilization of monomethyl sulfate by specialized methylotrophs. Experiencia 39:1257–1263
Harder W, Attwood MM (1978) Biology, physiology and biochemistry of hyphomicrobia. Adv Microb Physiol 17:303–359
Hirsch P (1974) Budding bacteria. Ann Rev Microbiol 28:391–444
Izumi Y, Takizawa M, Tani Y, Yamada H (1982) l-Serine production by resting cells of a methanol-utilizing bacterium. J Ferment Technol 60:269–276
Kanamaru K, Hieda T, Iwamuro Y, Mikami Y, Obi Y, Kisaki T (1981) Isolation and characterization of a Hyphomicrobium species and its polysaccharide formation from methanol. Agric Biol Chem 46:2411–2417
Miyazaki SS, Toki S, Izumi Y, Yamada H (1986a) Purification and characterization of a serine hydroxymethyltransferase from an obligate methylotroph, Hyphomicrobium methylovorum GM2. Eur J Biochem, (in press)
Miyazaki SS, Toki S, Izumi Y, Yamada H (1986b) Crystalline serine hydroxymethyltransferase from an obligate methylotroph, Hyphomicrobium methylovorum. Biochem Biophys Res Commun 139:71–79
Nakamura KD, Trewyn RW, Parks LW (1973) Purification and characterization of serine transhydroxymethylase from Saccharomyces cerevisiae. Biochim Biophys Acta 372:328–335
O'Connor ML, Hanson RS (1975) Serine transhydroxymethyltransferase isoenzymes from a facultative methylotroph. J Bacteriol 124:985–996
Ouchterlony O (1949) Antigen-antibody reactions in gels. Acta Pathol Microbiol Scand 26:507–515
Schirch L, Darrell P (1980) Purification and properties of mitochondrial serine hydroxymethyltransferase. J Biol Chem 255:7801–7806
Schirch L (1982) Serine hydroxymethyltransferase. In: Meister A (ed) Advances in enzymology, vol 53. Academic Press, New York, pp 83–112
Schirch L (1984) Folates in serine and glycine metabolism. In: Blakley RL, Benkovic SJ (eds) Folates and pterins, vol 1. Wiley Interscience, New York, pp, 399–455
Shishkina VN, Trotsenko YA (1974) Characteristic of a new Hyphomicrobium strain utilizing one-carbon compounds. Microbiology (English translation) 43:653–657
Stollar D, Levine L (1963) Two-dimensional immunodiffusion. In: Colowick SP, Kaplan MO (eds) Methods in enzymology, vol 6. Academic Press, New York, pp 848–854
Taylor RT, Weissbach H (1965) Radioactive assay for serine hydroxymethyltransferase. Anal Biochem 13:80–84
Uebayashi M, Tonomura K (1976) Denitrification by Hyphomicrobium capable of utilizing methanol. J Ferment Technol 54:885–890
Yamada H, Miyazaki SS, Izumi Y (1986) l-Serine production by a glycine-resistant mutant of ethylotrophic Hyphomicrobium methylovorum. Agric Biol Chem 50:17–21
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Miyazaki, S.S., Toki, Si., Izumi, Y. et al. Immunological characterization of serine hydroxymethyltransferase of methylotrophic Hyphomicrobium strains. Arch. Microbiol. 147, 328–333 (1987). https://doi.org/10.1007/BF00406128
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00406128