Zobrazeno 1 - 10
of 98
pro vyhledávání: '"Thomas A. Trautner"'
Publikováno v:
#N# Bacillus subtilis and Other Gram-Positive Bacteria
Several restriction/modification (R/M) systems have been identified in Bacillus subtilis and related bacteria and described in this chapter. Accepting the view that R/M systems have evolved to defend bacteria effectively against attack by bacterial v
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::55f30f25fefcdb802a3dd639f52346b3
https://doi.org/10.1128/9781555818388.ch38
https://doi.org/10.1128/9781555818388.ch38
Autor:
Anna S. Karyagina, Jörn Walter, M. V. Razumikhin, P. C. K. Lau, Thomas A. Trautner, Vorob'eva Ov, Elena A. Kubareva
Publikováno v:
Biochemistry (Moscow). 66:1356-1360
A method for determination of a non-methylated deoxycytidine (dC) residue in the recognition site of 5-cytosine DNA-methyltransferases is suggested. The method is based on treatment of methylated DNA by sodium bisulfite and successive reaction of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a15cd0b2dc98452d57894f7e0bfdb5a2
https://doi.org/10.1023/a:1013329728287
https://doi.org/10.1023/a:1013329728287
Autor:
Asita C. Stiege, Mário A. Santos, Anja Dröge, Juan C. Alonso, Rudi Lurz, Paulo Tavares, Thomas A. Trautner
Publikováno v:
Journal of Molecular Biology. 296:117-132
The procapsid of the Bacillus subtilis bacteriophage SPP1 is formed by the major capsid protein gp13, the scaffolding protein gp11, the portal protein gp6, and the accessory protein gp7. The protein stoichiometry suggests a T=7 symmetry for the SPP1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0898ac2a3892c3f3af2e396437044c56
https://doi.org/10.1006/jmbi.1999.3450
https://doi.org/10.1006/jmbi.1999.3450
Autor:
F. Zemlin, E. Beckmann, Rudi Lurz, Elena V. Orlova, Prakash Dube, Thomas A. Trautner, Paulo Tavares, Marin van Heel
Publikováno v:
Nature Structural Biology. 6:842-846
We have determined the three-dimensional structure of bacteriophage SPP1 portal protein (gp6) using electron microscopy at liquid-helium temperatures and angular reconstitution. The 13-fold symmetric gp6 oligomer is a turbine-shaped structure with th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c947b79af2783da2df38606ada07e75a
https://doi.org/10.1038/12303
https://doi.org/10.1038/12303
The complete nucleotide sequence and functional organization of Bacillus subtilis bacteriophage SPP1
Autor:
Sunghee Chai, Juan C. Alonso, Gerhild Lüder, Frank Weise, Asita C. Stiege, Thomas A. Trautner
Publikováno v:
Gene. 204:201-212
The complete nucleotide sequence of the B. subtilis bacteriophage SPP1 is described. The genome is 44 007 bp in size and has a base composition of 43.7% dG+dC. Only 32.2 kb are essential for phage amplification under laboratory conditions. Transcript
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ac6e0fd659ee6c313a57f1f38148afd
https://doi.org/10.1016/s0378-1119(97)00547-7
https://doi.org/10.1016/s0378-1119(97)00547-7
Autor:
Rudi Lurz, Dirk Günther, Thomas A. Trautner, Bernd Becker, Juan C. Alonso, Natalia de la Fuente, Paulo Tavares, Manuela Gassel
Publikováno v:
Journal of Molecular Biology. 268:822-839
We have identified and characterized the phage cistrons required for assembly of SPP1 heads. A DNA fragment containing most of the head morphogenesis genes was cloned and sequenced. The 3′-end of a previously identified gene (gene 6 ) and eight com
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c129779267417ecee2d75b53f3c29b1
https://doi.org/10.1006/jmbi.1997.0997
https://doi.org/10.1006/jmbi.1997.0997
Publikováno v:
Journal of Molecular Biology. 264:954-967
The virulent Bacillus subtilis bacteriophage SPP1 packages its DNA from a precursor concatemer by a headful mechanism. Following disruption of mature virions with chelating agents the chromosome end produced by the headful cut remains stably bound to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::73a3eab28e512321386a107fb7280443
https://doi.org/10.1006/jmbi.1996.0689
https://doi.org/10.1006/jmbi.1996.0689
Publikováno v:
The EMBO Journal. 15:1443-1450
In previous work on DNA-(cytosine-C5)-methyltransferases (C5-MTases), domains had been identified which are responsible for the sequence specificity of the different enzymes (target-recognizing domains, TRDs). Here we have analyzed the DNA methylatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07e5178e8b201e688d018e70ed5fbc8e
https://doi.org/10.1002/j.1460-2075.1996.tb00486.x
https://doi.org/10.1002/j.1460-2075.1996.tb00486.x
Publikováno v:
The EMBO Journal. 15:1434-1442
A large portion of the sequences of type II DNA-(cytosine-C5)-methyltransferases (C5-MTases) represent highly conserved blocks of amino acids. General steps in the methylation reaction performed by C5-MTases have been found to be mediated by some of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a9a5e6ad43363cdd99ac7425bfde837e
https://doi.org/10.1002/j.1460-2075.1996.tb00485.x
https://doi.org/10.1002/j.1460-2075.1996.tb00485.x
Publikováno v:
Nucleic Acids Research. 22:5517-5723
The temperate B.subtilis phages phi 3T and rho 11s code, in addition to the multispecific DNA (cytosine-C5) methyltransferases (C5-MTases) M. phi 3TI and M. rho 11sI, which were previously characterized, for the identical monospecific C5-MTases M. ph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3559ef6e79182027a3169b063cd567dd
https://doi.org/10.1093/nar/22.24.5517
https://doi.org/10.1093/nar/22.24.5517