Organization of multispecific DNA methyltransferases encoded by temperate Bacillus subtilis phages.

Behrens, B.; Noyer-Weidner, Mario; Pawlek, B.; Lauster, Roland; Balganesh, Tanjore S.; Trautner, Thomas A.

doi:10.1002/j.1460-2075.1987.tb04869.x

Cited by 72 publications

(49 citation statements)

References 25 publications

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“…4, lane D). (14), M -NgoII (GGCC) (27), M SinI (GGWCC) (9), M * Rholls (GGCC/GHGCDC) (2,29), and M. SPR (GGCC/CCGG/CCWGG) (8,18). The last two are encoded by Bacillus phages.…”

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confidence: 99%

Agmenellum quadruplicatum M.AquI, a novel modification methylase

Karreman¹,

Waard²

1990

J Bacteriol

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The complete type II modification methylase of Agmenellum quadruplicatum was cloned in Escherichia coli as an R Sau3A fragment of approximately 4.5 kilobases. The coding sequence was contained in a stretch of 1,156 base pairs which was organized into two parallel, partly overlapping open reading frames of 248 and 139 codons. In vivo complementation experiments showed that the synthesis of both predicted peptides was required for full methylase activity. The amino acid sequences were considerably similar to regions of other deoxycytidylate methylases.In procaryotic cells, two fundamentally different restriction-modification (R-M) systems have been found. They can be distinguished by their need for cofactors, as well as by their genetic organization. The R-M complex of the so-called type I systems requires S-adenosylmethionine, ATP, and Mg2+ for its functioning and contains the products of three genes: the first codes for the S unit, which recognizes the specific site, the second directs the synthesis of the R unit, which is responsible for cutting unmethylated DNA, and the last is translated into the M unit, which methylates non-or hemimethylated DNA. The absence of both of the protecting methyl groups at the recognition sites primes the R-M complex for attacking the DNA; the actual cleavage, however, does not occur at the recognition site itself, but somewhere else in the DNA molecule. The type II systems, on the other hand, code for two proteins: an endonuclease needing only Mg2+ for cleavage (which takes place at the recognition site itself) and a modification methylase requiring only S-adenosylmethionine for the protection of DNA. All type II systems characterized at the genetic level so far have been found to be encoded by just two genes: one for the endonuclease and another for the methylase. Only in the case of DpnII have two different methylase genes been discovered (3); both code for a protein that methylates independently of the other.In the cyanobacterium Agmenellum quadruplicatum, an R-M system that consists of isoschizomers of the AvaI (10,13)

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“…4, lane D). (14), M -NgoII (GGCC) (27), M SinI (GGWCC) (9), M * Rholls (GGCC/GHGCDC) (2,29), and M. SPR (GGCC/CCGG/CCWGG) (8,18). The last two are encoded by Bacillus phages.…”

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confidence: 99%

Agmenellum quadruplicatum M.AquI, a novel modification methylase

Karreman¹,

Waard²

1990

J Bacteriol

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“…In addition, the sequences from three GGCC-specific MTases from Bacillus subtilis phages SPR, 43T, and pll,S have been determined (1,41). This molecular characterization of GGCC-specific R/M systems allowed the identification of conserved sequence motifs such as the target-recognizing domains in the MTases and the study of the evolution of these proteins (1,(17)(18)(19)43).…”

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confidence: 99%

Characterization of the archaeal, plasmid-encoded type II restriction-modification system MthTI from Methanobacterium thermoformicicum THF: homology to the bacterial NgoPII system from Neisseria gonorrhoeae

Nölling¹,

Vos²

1992

J Bacteriol

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A restriction-modification system, designated MthTI, was localized on plasmid pFVI from the thermophilic archaeon Methanobacterium thermoformicicum THF. The MthTI system is a new member of the family of GGCC-recognizing restriction-modification systems. (18), with the exception of the pairs R.EcoRI-R.RsrI (36) and R.BsuFIRMspI (12). In contrast, considerable similarities between various MTases were found at the amino acid level, especially between those generating 5-methylcytosine (m CMTases) (15,19,26,37). Among R/M systems with m5C-

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“…(For such studies it is not necessary to have a sensitive host for the phage.) Some studies have already been reported for the psm DNA modification genes of the group III phages (G/inthert & Trautner, 1984;NoyerWeidner et al, 1985 ;Giinthert et al, 1986;Weiner, 1986;Gfinthert & Reiners, 1987;Behrens et al, 1987). …”

Section: Discussionmentioning

confidence: 96%

Genome Homology and Host Range of Some SPbeta-related Bacteriophages of Bacillus Subtilis and Bacillus amyloliquefaciens

Weiner

Zahler

1988

Journal of General Virology

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SUMMARYTemperate Bacillus subtilis bacteriophages SBfl, $3T and SPR and B. amyloliquefaciens phage H2 were compared with respect to DNA-DNA homology by Southern blot analysis to each other and to members of the genus Bacillus. The results show that H2 is a distantly related member of the group III B. subtilis phages. Detectable homology to group III phages could be found in the DNA of several other Bacillus species, including B. natto and B. amyloliquefaciens, demonstrating the widespread occurrence of this group of phages. The host ranges for the phages SPfl, SPR and H2 were determined by adsorption efficiency and by the ability of erythromycin resistance-and chloramphenicol resistance-transducing phages to convert susceptible host strains. Of the three phages examined, only H2 was capable of infecting B. amyloliquefaciens. Based on these results we propose that group III phages should be divided into three subgroups: SPfl, $3T, Rhol 1, IG1, IG3 and Z (subgroup 1), SPR (subgroup 2) and H2 (subgroup 3).

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Organization of multispecific DNA methyltransferases encoded by temperate Bacillus subtilis phages.

Cited by 72 publications

References 25 publications

Agmenellum quadruplicatum M.AquI, a novel modification methylase

Agmenellum quadruplicatum M.AquI, a novel modification methylase

Characterization of the archaeal, plasmid-encoded type II restriction-modification system MthTI from Methanobacterium thermoformicicum THF: homology to the bacterial NgoPII system from Neisseria gonorrhoeae

Genome Homology and Host Range of Some SPbeta-related Bacteriophages of Bacillus Subtilis and Bacillus amyloliquefaciens

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