Summary
Radioimmunoassay analysis of enteric and some other Gram-negative bacteria has shown that the antigenic structure of the RNA polymerase α subunit is more conserved than that of the β and β' subunits. Since anti-α antibodies do not affect RNA polymerase activity, the constrains which determine the low variability of the antigenic structure of the α subunit are not directly related to its functional role. The antigenic determinants of the α subunit located on the surface of the RNA polymerase molecule are more conserved than those involved in contacts with other subunits; an opposite tendency characterizes the β subunit. The range of variability of the antigenic determinants buried inside the RNA polymerase molecule suggests that the subunits are attached to each other rather loosely. Immunological comparison of RNA polymerases provides a simple method for reconstructing bacterial genealogies. The genealogy of the bacteria examined is essentially in agreement with phylogenetic trees based on 16S and 5S rRNA sequence characterization. This argues against extensive interspecific transfer of genes coding for components of the transcription and translation apparatus.
Similar content being viewed by others
References
Bradferd MM (1976) A rapid and sensitive method for the quantitition of microgram quantities of protein utilising the principle of proteindye binding. Analyt Biochem 72:248–254
Burgess RR, Jendrisak JJ (1975) A procedure for the rapid, large-scale purification of E. coli RNA polymerase involving Polymin P precipitation and DNA-cellulose chromatography. Biochemistry 14:4634–4639
Cocks GT, Wilson AC (1972) Enzyme evolution in the Enterobacteriaceae. J Bacteriol 110:793–802
Fox GE, Stackebrandt E, Hespell RB, Gibson J, Maniloff J, Dyer TA, Wolfe RS, Balch WE, Tanner RS, Magrum LJ, Zablen LB, Blakemore R, Gupta R, Bonen L, Lewis BJ, Stahl DA, Luehrsen KR, Chen KN, Woese CR (1980) The phylogeny of prokaryotes. Science 209:457–463
Gragerov AI, Nikiforov VG (1980) Conserved antigenic determinants in the vicinity of the DNA-binding center of bacterial RNA polymerase. FEBS Lett 122:17–20
Gurvich AE, Kusovleva OB, Tumanova AE (1961) Production of protein-cellulose complexes (immunosorbents) in the form of suspensions able to bind great amounts of antibodies. Biokhimiya 26:334–342
Heil A, Zillig W (1970) Reconstruction of bacterial DNA-dependent RNA polymerase from isolated subunits as a tool for the elucidation of the role of the subunits in transcription. FEBS Lett 11:165–168
Hofstra H, Dankert J (1980) Major outer membrane proteins: common antigens in Enterobacteriaceae species. J Gen Microbiol 119:123–131
Hori H, Osawa S (1980) Recent studies on the evolution of 5S RNA. In: Osawa S, Ozeki H, Uchida H, Yura T (eds) Genetics and evolution of RNA polymerase tRNA and ribosomes. Univ. of Tokyo Press, Tokyo, pp 539–551
Kimura M (1980) Contribution of population genetics to molecular evolutionary studies. In: Osawa S, Ozeki H, Uchida H, Yura T (eds) Genetics and evolution of RNA polymerase, tRNA and ribosomes. Univ. of Tokyo Press, Tokyo, pp 499–518
Lill UI, Behrendt EM, Hartmann GR (1975) Hybridization in vitro of subunits of the DNA-dependent RNA polymerase from Escherichia coli and Microccoccus luteus. Eur J Biochem 52:411–420
Lipkin VM, Modyanov NN, Kocherginskaya SA, Chertov OYu, Nikiforov VG, Lebedev AN (1976) Comparative study of the peptide maps of the RNA polymerase α subunits of bacteria of the family Enterobacteriaceae. Bioorgan Khimiya 2:1174–1181
Lipkin VM, Modyanov NN, Chertov OYu, Kocherginskaya SA, Nikiforov VG, Lebedev AN (1979) Modification of tyrosine residues in DNA-dependent RNA polymerase from E. coli. Bioorgan Khimiya 5:929–936
Lowe PA, Malcolm ADB (1976) Structural properties of Escherichia coli RNA polymerase subunits. Eur J Biochem 64:177–188
Nakamura K, Pirtle RM, Inouye M (1979) Homology of the gene coding for outer membrane lipoprotein within various Gram-negative bacteria. J Bacteriol 137:595–604
Nikiforov VG (1971) Hybrid RNA polymerases formed from core enzyme and sigma factors of E. coli and thermophilic B. megaterium. FEBS Lett 16:74–76
Piepersberg A, Hennecke H, Engelhard M, Nass G, Bock A (1975) Gross-reactivity of phenylalanyl-transfer ribonucleic acid ligases from different microorganisms. J Bacteriol 124:1482–1488
Reyes GR, Rocha V (1977) Immunochemical comparison of phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase among the Enterobacteriaceae. J Bacteriol 129:1448–1456
Saitoh T, Ishihama A (1976) Subunits of RNA polymerase in function and structure VI. Sequence of the assembly in vitro of Escherichia coli RNA polymerase. J Mol Biol 104:621–635
Stanier RY, Adelberg EA, Ingraham JL (1976) The microbiol world. Prentice-Hall, Inc., Engelewood Cliffs, New Jersey, Chapter 20
Stoffler G, Wool IG, Lin A, Rak KH (1974) The identification of the eukaryotic ribosomal proteins homologous with Escherichia coli proteins L7 and L12. Proc Natl Acad Sci USA 71:4723–4726
Tafler SW, Setlow P, Levine L. Serological relatedness of bacterial deoxyribonucleic acid polymerases. J Bacteriol 113:18–23
Whitely HR, Hemphill HE (1970) The interchangeability of stimulatory factors isolated from three microbial RNA polymerases. Biochem Biophys Res Commun 41:647–654
Wiggs JL, Bush JW, Chamberlin MJ (1979) Utilization of promoter and terminator sites on bacteriophage T7 DNA by RNA polymerases from a variety of bacterial orders. Cell 16:97–109
Yamada T, Murooka Y, Harada T (1978) Comparative immunological studies on arylsulfatase in bacteria of the family Enterobacteriaceae: occurrence of latent arylsulfatase protein regulated by sulfur compounds and tyramine. J Bacteriol 133:536–541
Zimmer SG, Millette RL (1979) DNA-dependent RNA polymerase from Pseudomonas BAL-31. Effect of σ and template homology on the stimulation and selectivity of transcription. J Biol Chem 254:2199–2204
Author information
Authors and Affiliations
Additional information
Communicated by D. Goldfarb
Rights and permissions
About this article
Cite this article
Nikiforov, V.G., Lebedev, A.N. & Kalyaeva, E.S. Antigenic variability of bacterial RNA polymerases. Molec. Gen. Genet. 183, 518–521 (1981). https://doi.org/10.1007/BF00268774
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00268774