Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
TOL PLASMID TRANSCRIPTION FACTOR XYLS BINDS SPECIFICALLY TO THE PM OPERATOR SEQUENCE
Autore:
KALDALU N; MANDEL T; USTAV M;
Indirizzi:
TARTU STATE UNIV,INST MOLEC & CELL BIOL,DEPT MICROBIOL & VIROL,23 RIIA ST EE-2400 TARTU ESTONIA TARTU STATE UNIV,INST MOLEC & CELL BIOL,DEPT MICROBIOL & VIROL EE-2400 TARTU ESTONIA ESTONIAN BIOCTR EE-2400 TARTU ESTONIA
Titolo Testata:
Molecular microbiology
fascicolo: 3, volume: 20, anno: 1996,
pagine: 569 - 579
SICI:
0950-382X(1996)20:3<569:TPTFXB>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-DNA RECOGNITION; META-CLEAVAGE PATHWAY; COLI RNA-POLYMERASE; ESCHERICHIA-COLI; ARAC-PROTEIN; POSITIVE REGULATOR; MOLECULAR CHAPERONES; PSEUDOMONAS-PUTIDA; PROMOTER; CONTACTS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
56
Recensione:
Indirizzi per estratti:
Citazione:
N. Kaldalu et al., "TOL PLASMID TRANSCRIPTION FACTOR XYLS BINDS SPECIFICALLY TO THE PM OPERATOR SEQUENCE", Molecular microbiology, 20(3), 1996, pp. 569-579

Abstract

XyIS, an AraC family transcription factor, positively regulates transcription of Pseudomonas putida TOL plasmid meta operon from the Pm promoter. A tandem of 15 bp homologous direct repeats, separated by 6 bp and overlapping with the -35 hexamer of the promoter, is required for the activation of Pm by XyIS in vivo. In this study we have characterized specific binding of XyIS to the Pm operator Om. XyIS was overexpressed with an epitope tag in its N-terminus. Tagged XyIS (N-XyIS) was immunopurified and was shown to specifically bind to Om. We have used matrix-bound N-XyIS in DNA footprinting and methylation interference experiments. Binding of N-XyIS protects 44 bp in the Om region on both strands from DNase I digestion and generates hypersensitive sites (within the protected area) which lie on the same face of the DNA helix. Results of hydroxyl radical footprinting and methylation interference assays indicate that XyIS binds along one side of the DNA and covers four helical turns. The protein has base-specific contacts in four adjacent major groove regions on the same helical face. Our data are in accord with the prediction of the presence of two separate DNA-binding units in an XyIS molecule which are involved in base-specific contacts intwo adjacent major-groove regions of a half-site. The direct repeat arrangement of the binding site and the mode of DNA binding of XyIS aresimilar to the arrangement of recognition sites and the DNA contact pattern of AraC protein from Escherichia coil.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/09/20 alle ore 22:36:57