jeanflop/post-ocr-correction huggingface dataset:
Y., Watanabe T. 1978. Distribution of AMP-deaminase isozymes in rat tissues. Eur. J. Biochem. 87: 297-304. Solano C, Coffee C. J. 1978. Differential responses of AMP deaminase isozymes to changes in the adenylate energy charge. Biochem. Biophys. Res. Commun. 85: 564-71. Morisaki T., Sabina R. L, Holmes E. W. 1990. Adenylate deaminase. A multigene family in humans and rats. J. Biol. Chem. 265: 11482-6. Sabina R. L., Morisaki T., Clarke P., Eddy R., Shows T. B., Morton C, Holmes E. W. 1990. Characterization of the human and rat myoadenylate deaminase. J. Biol. Chem. 265: 9423-33. Mahnke-Zizelman D. K., Sabina R.
J. Biol. Chem. 265: 9423-33. Mahnke-Zizelman D. K., Sabina R. L. 1992. Cloning of human AMP deaminase isoform E cDNAs: evidence for a third AMP deaminase gene exhibiting alternatively spliced 5'-exons. J. Biol. Chem. 267: 20866-77. Makarewicz W., Zydowo M. 1962. Comparative studies on some ammonia-producing enzymes in the excretory organs of vertebrates. Comp. Biochem. Physiol. 6: 269-75. Makarewicz W. 1963. AMP-aminohydrolase and glutaminase activities in the kidneys and gills of some freshwater vertebrates. Acta Biochim. Polon. 10: 363-9. Fijisawa K., Yoshino M. 1987. Activities of adenylate-degrading enzymes in muscles from vertebrates and invertebrates. Comp. Biochem. Physiol. 86B: 109-12. Lazou
from vertebrates and invertebrates. Comp. Biochem. Physiol. 86B: 109-12. Lazou A. 1989. Adenylate metabolizing enzymes in invertebrate tissues. Comp. Biochem. Physiol. 92B: 175-80. Raffin J.-P., Thébault M.-T. 1991. A specific AMP deaminase assay and its application to tissue homogenates. Comp. Biochem. Physiol. 99B: 125-7. Raffin J.-P., Izem L., Thébault M.-T. 1993. Amplification of myoadenylate deaminase during evolution. 2. Purification and properties of the enzyme from two elasmobranch fishes, Scyliorhinus canicula and Raja clavata. Comp. Biochem. Physiol. 106B: 999-1007. Bone Q. 1978. Locomotor muscle. In: Hoar W. S., Randall D. J., eds. Fish physiology, vol. 7. New York: Academic Press, 361-424.
eds. Fish physiology, vol. 7. New York: Academic Press, 361-424. Nisbet R. H., Plummer J. M. 1968. The fine structure of cardiac and other molluscan muscle. In: Fretter V., ed. Symposia of the Zoological Society of London: studies in the structure, physiology and ecology of molluscs. New York: Academic Press, 193-211. Wiersma C. G. A. 1961. The neuromuscular System. In: Waterman T. H., ed. The physiology of Crustacea, vol. 2. New York: Academic Press, 191-240. Jahromi S. S., Atwood H. L. 1969. Correlation of structure, speed of contraction, and total tension in fast and slow abdominal muscle fibers of the
tension in fast and slow abdominal muscle fibers of the lobster (Homarus americanus). J. Exp. Zool. 171: 25-38. Prenant M. 1929. Recherches sur la structure des muscles des Annélides Polychètes. Arch. Zool. Exp. Cen. 69: 1-135. Olsson M. 1940. Histology of the retractor muscles of Phascolosoma gouldii. Biol. Bull. 78: 24. Ashby B., Frieden C 1977. Interaction of AMP-aminohydrolase with myosin and its subfragments. J. Biol. Chem. 252: 1869-72. Shiraki H., Ogawa H., Matsuda Y., Nakagawa H. 1979. Interaction of rat muscle AMP deaminase with myosin. I. Biochemical study of the interaction of AMP deaminase and myosin in rat muscle.
the interaction of AMP deaminase and myosin in rat muscle. Biochim. Biophys. Acta 566: 335-44. C. R. Acad. Sci. Paris, Sciences de la vie/Life sciences, 1994; 317: 386-91 Amplification of myoadenylate deaminase during evolution 26. Smiley K. L, Berry A. J., Suelter C. H. 1967. An improved purification, crystallization, and some properties of rabbit muscle 5'-adenylic acid deaminase. J. Biol. Chem. 242: 2502-6. 27. Raffin J.-P., Thébault M.-T. 1987. Purification and partial characterization of an AMP deaminase from the marine invertebrate Palaemon serratus. Comp. Biochem. Physiol. 88B: 1071-6. 28. Kalckar H. M. 1947. Differential spectrometry of purine compounds by means
H. M. 1947. Differential spectrometry of purine compounds by means of specific enzymes. I. Determination of adenine compounds. J. Biol. Chem. 167: 445-60. 29. Stankiewicz A. 1983. Direct deamination of AMP, ADP, ATP and NADH by a non-specific adenylate deaminase in the foot muscle of the snail Helix pomatia. Biochem. J. 215: 39-44. 30. Kaletha K., Thébault M.-T., Raffin J.-P. 1991. Comparative studies on heart and skeletal muscle AMP-deaminase from rainbow trout (Salmo gairdneri). Comp. Biochem. Physiol. 99B: 751-4. 31. Ohno S., Muramoto J., Stenius C, Christian L., Kittrell W. A., Atkin N. B. 1969. Microchromosomes in Holocephalian, Chondrostean and
A., Atkin N. B. 1969. Microchromosomes in Holocephalian, Chondrostean and Holostean fishes. Chromosoma (Berl.) 26: 35-40. 32. Raffin J.-P., Leroy J. P., Izem L, Thébault M.-T. 1994. A histochemical study of elasmobranch fish musculature: evidence for structural changes between Squalidae and Rajidae related to evolution in higher vertebrates. In préparation. 33. Debatisse M., De Saint-Vincent B. R., Buttin G. 1984. Expression of several amplified genes in an adenylate-deaminase overproducing variant of chinese hamster fibroblasts. EMBO J. 3: 3123-7. 34. Debatisse M., Saito I., Buttin G., Stark G. R. 1988. Preferential amplification of rearranged sequences near amplified adenylate deaminase gene. Mol.
amplification of rearranged sequences near amplified adenylate deaminase gene. Mol. Cell. Biol. 8: 17-24. 35. Nelson J. S. 1984. Fishes of the world, 2nd ed. New York: John Wiley and Sons. 36. Nelson G. 1989. Phylogeny of major fish groups. In: Fernholm B., Bremer K., Brundin L, Jörgvall H., Rutberg L, Wanntorp H. E., eds. The hierarchy of life. Molecules and morphology in phylogenetic analysis. Amsterdam: Excerpta Medica, 325-36. C. R. Acad. Sci. Paris, Sciences de la vie/Life sciences, 1994; 317: 386-91 392 Biologie et génétique moléculaire/Molecular biology and genetics RÉSUMÉ Le génome de Spiroplasma melliferum, souche BC-3, a été
RÉSUMÉ Le génome de Spiroplasma melliferum, souche BC-3, a été cartographié au moyen de la technique d'électrophorèse en champ pulvérisé et avec l'aide de plusieurs enzymes de restriction. Plusieurs marqueurs génétiques ont été localisés sur la carte. Le chromosome de S. melliferum contient aussi de nombreuses séquences homologues à celles de deux viruses SpV1 (virus de spiroplasme). La taille du génome de S. melliferum est de 360 kpb inférieure à celle de Spiroplasma citri, souche R8A2-HP. Les génomes de deux spiroplasmes ont des organisations similaires, avec néanmoins des indications de réarrangements chromosomiques. Mots clés: Spiroplasma melliferum, Spiroplasma citri, carte génomique.
réarrangements chromosomiques. Mots clés: Spiroplasma melliferum, Spiroplasma citri, carte génomique. ### CORRECTION ### Kawamura Y., Yoshino M. 1974. Multiple forms of AMP deaminase in various tissues. FEBS Lett. 44: 63-6. Ogasawara N., Goto H., Yamada Y., Watanabe T. 1978. Distribution of AMP-deaminase isozymes in rat tissues. Eur. J. Biochem. 87: 297-304. Solano C, Coffee C. J. 1978. Differential responses of AMP deaminase isozymes to changes in the adenylate energy charge. Biochem. Biophys. Res. Commun. 85: 564-71. Morisaki T., Sabina R. L, Holmes E. W. 1990. Adenylate deaminase. A multigene family in humans and rats. J. Biol. Chem. 265: 11482-6. Sabina
in humans and rats. J. Biol. Chem. 265: 11482-6. Sabina R. L., Morisaki T., Clarke P., Eddy R., Shows T. B., Morton C, Holmes E. W. 1990. Characterization of the human and rat myoadenylate deaminase. J. Biol. Chem. 265: 9423-33. Mahnke-Zizelman D. K., Sabina R. L. 1992. Cloning of human AMP deaminase isoform E cDNAs: evidence for a third AMP deaminase gene exhibiting alternatively spliced 5'-exons. J. Biol. Chem. 267: 20866-77. Makarewicz W., Zydowo M. 1962. Comparative studies on some ammonia-producing enzymes in the excretory organs of vertebrates. Comp. Biochem. Physiol. 6: 269-75. Makarewicz W. 1963. AMP-aminohydrolase and glutaminase activities
Physiol. 6: 269-75. Makarewicz W. 1963. AMP-aminohydrolase and glutaminase activities in the kidneys and gills of some freshwater vertebrates. Acta Biochim. Polon. 10: 363-9. Fijisawa K., Yoshino M. 1987. Activities of adenylate-degrading enzymes in muscles from vertebrates and invertebrates. Comp. Biochem. Physiol. 86B: 109-12. Lazou A. 1989. Adenylate metabolizing enzymes in invertebrate tissues. Comp. Biochem. Physiol. 92B: 175-80. Raffin J.-P., Thébault M.-T. 1991. A specific AMP deaminase assay and its application to tissue homogenates. Comp. Biochem. Physiol. 99B: 125-7. Raffin J.-P., Izem L., Thébault M.-T. 1993. Amplification of myoadenylate deaminase during evolution. 2. Purification and properties of the enzyme from
during evolution. 2. Purification and properties of the enzyme from two elasmobranch fishes, Scyliorhinus canicula and Raja clavata. Comp. Biochem. Physiol. 106B: 999-1007. Bone Q. 1978. Locomotor muscle. In: Hoar W. S., Randall D. J., eds. Fish physiology, vol. 7. New York: Academic Press, 361-424. Nisbet R. H., Plummer J. M. 1968. The fine structure of cardiac and other molluscan muscle. In: Fretter V., ed. Symposia of the Zoological Society of London: studies in the structure, physiology and ecology of molluscs. New York: Academic Press, 193-211. Wiersma C. G. A. 1961. The neuromuscular System. In: Waterman T. H., ed. The
1961. The neuromuscular System. In: Waterman T. H., ed. The physiology of Crustacea, vol. 2. New York: Academic Press, 191-240. Jahromi S. S., Atwood H. L. 1969. Correlation of structure, speed of contraction, and total tension in fast and slow abdominal muscle fibers of the lobster (Homarus americanus). J. Exp. Zool. 171: 25-38. Prenant M. 1929. Recherches sur la structure des muscles des Annélides Polychètes. Arch. Zool. Exp. Cen. 69: 1-135. Olsson M. 1940. Histology of the retractor muscles of Phascolosoma gouldii. Biol. Bull. 78: 24. Ashby B., Frieden C 1977. Interaction of AMP-aminohydrolase with myosin and its subfragments. J.
1977. Interaction of AMP-aminohydrolase with myosin and its subfragments. J. Biol. Chem. 252: 1869-72. Shiraki H., Ogawa H., Matsuda Y., Nakagawa H. 1979. Interaction of rat muscle AMP deaminase with myosin. I. Biochemical study of the interaction of AMP deaminase and myosin in rat muscle. Biochim. Biophys. Acta 566: 335-44. C. R. Acad. Sci. Paris, Sciences de la vie/Life sciences, 1994; 317: 386-91 Amplification of myoadenylate deaminase during evolution 26. Smiley K. L, Berry A. J., Suelter C. H. 1967. An improved purification, crystallization, and some properties of rabbit muscle 5'-adenylic acid deaminase. J. Biol. Chem. 242: 2502-6. 27. Raffin
5'-adenylic acid deaminase. J. Biol. Chem. 242: 2502-6. 27. Raffin J.-P., Thébault M.-T. 1987. Purification and partial characterization of an AMP deaminase from the marine invertebrate Palaemon serratus. Comp. Biochem. Physiol. 88B: 1071-6. 28. Kalckar H. M. 1947. Differential spectrometry of purine compounds by means of specific enzymes. I. Determination of adenine compounds. J. Biol. Chem. 167: 445-60. 29. Stankiewicz A. 1983. Direct deamination of AMP, ADP, ATP and NADH by a non-specific adenylate deaminase in the foot muscle of the snail Helix pomatia. Biochem. J. 215: 39-44. 30. Kaletha K., Thébault M.-T., Raffin J.-P. 1991. Comparative studies on heart
K., Thébault M.-T., Raffin J.-P. 1991. Comparative studies on heart and skeletal muscle AMP-deaminase from rainbow trout (Salmo gairdneri). Comp. Biochem. Physiol. 99B: 751-4. 31. Ohno S., Muramoto J., Stenius C, Christian L., Kittrell W. A., Atkin N. B. 1969. Microchromosomes in Holocephalian, Chondrostean and Holostean fishes. Chromosoma (Berl.) 26: 35-40. 32. Raffin J.-P., Leroy J. P., Izem L, Thébault M.-T. 1994. A histochemical study of elasmobranch fish musculature: evidence for structural changes between Squalidae and Rajidae related to evolution in higher vertebrates. In préparation. 33. Debatisse M., De Saint-Vincent B. R., Buttin G. 1984. Expression of several amplified genes
B. R., Buttin G. 1984. Expression of several amplified genes in an adenylate-deaminase overproducing variant of chinese hamster fibroblasts. EMBO J. 3: 3123-7. 34. Debatisse M., Saito I., Buttin G., Stark G. R. 1988. Preferential amplification of rearranged sequences near amplified adenylate deaminase gene. Mol. Cell. Biol. 8: 17-24. 35. Nelson J. S. 1984. Fishes of the world, 2nd ed. New York: John Wiley and Sons. 36. Nelson G. 1989. Phylogeny of major fish groups. In: Fernholm B., Bremer K., Brundin L, Jörgvall H., Rutberg L, Wanntorp H. E., eds. The hierarchy of life. Molecules and morphology in phylogenetic analysis.
The hierarchy of life. Molecules and morphology in phylogenetic analysis. Amsterdam: Excerpta Medica, 325-36. C. R. Acad. Sci. Paris, Sciences de la vie/Life sciences, 1994; 317: 386-91 392 Biologie et génétique moléculaire/Molecular biology and genetics RÉSUMÉ Le génome de Spiroplasma melliferum, souche BC-3, a été cartographié au moyen de la technique d'électrophorèse en champ pulvérisé et avec l'aide de plusieurs enzymes de restriction. Plusieurs marqueurs génétiques ont été localisés sur la carte. Le chromosome de S. melliferum contient aussi de The genome of Spiroplasma melliferum, strain BC-3, has been physically mapped by pulsed field gel electrophoresis of DNA cleaved by
mapped by pulsed field gel electrophoresis of DNA cleaved by various restriction enzymes. Southern hybridization has been used to localize several genetic loci. Multiple regions homologous to the sequences of two Spiroplasma viruses have also been localized. The genome of S. melliferum is some 360 kbp shorter than that of Spiroplasma citri, strain R8A2 HP. The overall genetic organization of the two Spiroplasma species is fairly well conserved, but there are indications of chromosome rearrangements. Key words: Spiroplasma melliferum, Spiroplasma citri, genomic map. Voir Version abrégée (p. 397) Spiroplasmas are wall-less eubacteria characterized by helical morphology and motility in liquid
wall-less eubacteria characterized by helical morphology and motility in liquid medium. They have a small genome with low guanine plus cytosine (G+C) content (24-31 mol %). They are members of a single genus, Spiroplasma, in the family Spiroplasmataceae, order Entomoplasmatales, class Mollicutes [1]. More than 250 different spiroplasma isolates have been recovered from plants and arthropods, including many insects. According to the similarities of their genomic DNA sequences and their serological relationships, the isolates have been classified into 24 groups [2]. Spiroplasma citri, the causal agent of citrus stubborn disease and the first spiroplasma to have been cultured [3], belongs
and the first spiroplasma to have been cultured [3], belongs to group 1, the S. citri group. This group is divided into 8 subgroups, among which Spiroplasma melliferum (subgroup 1-2), Spiroplasma kunkelii (subgroup 1-3) and Spiroplasma phoeniceum (subgroup 1-8) share extensive similarities in DNA sequences with S. citri (subgroup 1-1), respectively 68 %, 57 % and 60 % [4]. S. citri, S. phoeniceum and S. kunkelii are the only known plant pathogenic spiroplasmas, while S. melliferum is a honeybee pathogen [5]. Bacteria exchange genetic material by conjugation during mating. This phenomenon was used in the 1950s to initiate the genetic
phenomenon was used in the 1950s to initiate the genetic map of Escherichia coli [6]. Similar studies have not been undertaken in the mollicutes as conjugation has never been shown to occur in these organisms. Note présentée par Joseph Marie Bové. Note remise le 8 novembre 1993, acceptée après révision le 11 avril 1994. 392 Spiroplasma melliferum genomic map Recently, however, pulsed-field gel electrophoresis (PFGE), a technique by which very large DNA fragments can be separated, has made it possible not only to accurately determine genome sizes, but also to construct genomic maps by combining PFGE with molecular hybridization. It
construct genomic maps by combining PFGE with molecular hybridization. It could be demonstrated that the genome sizes of mollicutes were variable within the same genus and even species, and that genome size could not be taken, anymore, as a taxonomic criterion [7-9]. For instance, S. citri strain R8A2-HP has a genome size of 1 820 kbp, but recent studies have shown that, inside spiroplasma group I, genome sizes range from 1460 kbp to 2 200 kbp [10]. Using PFGE, the physical and genomic maps of several mollicutes have been established and several known genes have been located on these maps
and several known genes have been located on these maps [11-19]. We have recently established a physical and genomic map of S. citri and this map is among those with the greatest number of identified loci in the mollicutes [19]. Because S. melliferum has the highest genomic similarity with S. citri, we have constructed its physical and genomic map and have compared it with that of S. citri. Materials and methods Preparation and separation of restriction fragments S. melliferum BC-3 (ATCC 33219) [20] was grown in BSR medium at 32 °C [21]. Genomic DNA was prepared after inclusion of pellets
°C [21]. Genomic DNA was prepared after inclusion of pellets of the organisms in Low Melting Point (LMP) agarose plugs as previously described [19]. The genomic DNA was subsequently digested with restriction enzymes ApaI, BssHII, and SauI (Gibco-BRL, New England Biolabs), and separated in 1 % agarose gel using pulsed field gel electrophoresis (PFGE) (TAFE System, Geneline TM II, Beckman), with 3 steps, each of 12 h, with pulse times of 60, 120, and 180 s, respectively, at an amperage of 370 mA, in 0.25X TBE buffer, at 8°C. The size of the separated fragments was evaluated by comparison with
size of the separated fragments was evaluated by comparison with Saccharomyces cerevisiae chromosomal DNAs (Biorad). Hybridization procedures After staining with ethidium bromide and photography under UV light, the agarose gels were treated twice for 10 min with 0.25 N HCl. Then the DNA fragments were transferred onto Hybond N+ nylon membranes (Amersham) according to the standard Southern blot procedure, using the alkaline method [22, 23]. The DNA fragments used as probes in hybridization experiments are listed in Table I. They were labeled from α-32P-dATP, using the random primer labeling kit from Gibco-BRL. Hybridizations were carried out at 42 °C in
from Gibco-BRL. Hybridizations were carried out at 42 °C in a buffer containing 50 % formamide and washes were performed at 50 °C, twice 10 min in 2XSSC, 0.1 % SDS, twice 15 min in 0.1 X SSC, 0.1 % SDS, and twice 5 min in 2X SSC. Results and discussion The restriction fragments separated by PFGE are shown in Figure 1 and summarized in Table II. The genome size obtained by summing up the values of the individual restriction fragments is close to 1 460 kbp. The physical maps for enzymes ApaI, BssHII and SauI have been established from
for enzymes ApaI, BssHII and SauI have been established from reciprocal double digestion products according to the method of Bautsch [11], as already described for the S. citri map [19]. Southern blot analyses were carried out with the probes listed in Table I. As an illustration, the results obtained with fib and pyrG-purA-purB as the probes are shown in Figure 2. The linearized physical and genomic map of S. melliferum is shown in Figure 3. Table I Genes used as probes for the establishment of S. melliferum genomic map Gene(s) Product(s) Source Reference rpsB-tsf-x-spi Ribosomal protein S2, Elongation factor Ts,
Product(s) Source Reference rpsB-tsf-x-spi Ribosomal protein S2, Elongation factor Ts, protein X, Spiralin S. citri [24] 6-phosphofructokinase, Pyruvate kinase fibrillar protein S. citri [25] Elongation factor Tu M. gallisepticum [26] CTP synthetase, Adenylosuccinate synthetase and lyase S. citri [27] RNA polymerase α subunit S. citri [28] valine tRNA synthetase S. citri [28] DNA replication protein A, S. citri [29] Chromosomal replication origin rRNA 16S S. citri [30] trpJ-trpU-ser1 tRNAs Trp(UCA), Trp(CCA), Ser(CGA) S. 392 ### CORRECTION ### The genome of Spiroplasma melliferum, strain BC-3, has been physically mapped by pulsed field gel electrophoresis of DNA cleaved by various restriction enzymes.
field gel electrophoresis of DNA cleaved by various restriction enzymes. Southern hybridization has been used to localize several genetic loci. Multiple regions homologous to the sequences of two Spiroplasma viruses have also been localized. The genome of S. melliferum is some 360 kbp shorter than that of Spiroplasma citri, strain R8A2 HP. The overall genetic organization of the two Spiroplasma species is fairly well conserved, but there are indications of chromosome rearrangements. Key words: Spiroplasma melliferum, Spiroplasma citri, genomic map. Voir Version abrégée (p. 397) Spiroplasmas are wall-less eubacteria characterized by helical morphology and motility in liquid medium. They have
by helical morphology and motility in liquid medium. They have a small genome with low guanine plus cytosine (G+C) content (24-31 mol %). They are members of a single genus, Spiroplasma, in the family Spiroplasmataceae, order Entomoplasmatales, class Mollicutes [1]. More than 250 different spiroplasma isolates have been recovered from plants and arthropods, including many insects. According to the similarities of their genomic DNA sequences and their serological relationships, the isolates have been classified into 24 groups [2]. Spiroplasma citri, the causal agent of citrus stubborn disease and the first spiroplasma to have been cultured [3], belongs to group 1,
spiroplasma to have been cultured [3], belongs to group 1, the S. citri group. This group is divided into 8 subgroups, among which Spiroplasma melliferum (subgroup 1-2), Spiroplasma kunkelii (subgroup 1-3) and Spiroplasma phoeniceum (subgroup 1-8) share extensive similarities in DNA sequences with S. citri (subgroup 1-1), respectively 68 %, 57 % and 60 % [4]. S. citri, S. phoeniceum and S. kunkelii are the only known plant pathogenic spiroplasmas, while S. melliferum is a honeybee pathogen [5]. Bacteria exchange genetic material by conjugation during mating. This phenomenon was used in the 1950s to initiate the genetic map of Escherichia
in the 1950s to initiate the genetic map of Escherichia coli [6]. Similar studies have not been undertaken in the mollicutes as conjugation has never been shown to occur in these organisms. Note présentée par Joseph Marie Bové. Note remise le 8 novembre 1993, acceptée après révision le 11 avril 1994. 392 Spiroplasma melliferum genomic map Recently, however, pulsed-field gel electrophoresis (PFGE), a technique by which very large DNA fragments can be separated, has made it possible not only to accurately determine genome sizes, but also to construct genomic maps by combining PFGE with molecular hybridization. It could be demonstrated
by combining PFGE with molecular hybridization. It could be demonstrated that the genome sizes of mollicutes were variable within the same genus and even species, and that genome size could not be taken, anymore, as a taxonomic criterion [7-9]. For instance, S. citri strain R8A2-HP has a genome size of 1 820 kbp, but recent studies have shown that, inside spiroplasma group I, genome sizes range from 1460 kbp to 2 200 kbp [10]. Using PFGE, the physical and genomic maps of several mollicutes have been established and several known genes have been located on these maps [11-19]. We have
genes have been located on these maps [11-19]. We have recently established a physical and genomic map of S. citri and this map is among those with the greatest number of identified loci in the mollicutes [19]. Because S. melliferum has the highest genomic similarity with S. citri, we have constructed its physical and genomic map and have compared it with that of S. citri. Materials and methods Preparation and separation of restriction fragments S. melliferum BC-3 (ATCC 33219) [20] was grown in BSR medium at 32 °C [21]. Genomic DNA was prepared after inclusion of pellets of the organisms