Literature DB >> 2254930

FLP protein of 2 mu circle plasmid of yeast induces multiple bends in the FLP recognition target site.

C J Schwartz1, P D Sadowski.   

Abstract

The FLP recombinase of the 2 mu plasmid of Saccharomyces cerevisiae binds to a target containing three 13 base-pair symmetry elements called a, b and c. The symmetry elements b and c are in direct orientation while the a element is in inverted orientation with respect to b and c on the opposite side of an eight base-pair core region. Each symmetry element acts as a binding site for the FLP protein. The FLP protein can form three different complexes with the FLP recognition target (FRT site) according to the number of elements within the site that are occupied by the FLP protein. Binding of FLP to the FRT site induces DNA bending. We have measured the angles of bends caused by the binding of the FLP protein to full and partial FRT sites. We find that FLP induces three types of bend in the FRT-containing DNA. The type I bend is approximately 60 degrees and results from a molecule of FLP bound to one symmetry element. The type II bend is greater than 144 degrees and results from FLP molecules bound to symmetry elements a and b. The type III bend is approximately 65 degrees and results from FLP proteins bound to symmetry elements b and c. Certain FLP proteins that are defective in recombination can generate the type I and type III bends but are impaired in their ability to induce the type II bend. We discuss the role of bending in FLP-mediated recombination.

Entities:  

Mesh:

Substances:

Year:  1990        PMID: 2254930     DOI: 10.1016/s0022-2836(05)80320-1

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  14 in total

1.  The FLP protein contacts both major and minor grooves of its recognition target sequence.

Authors:  G B Panigrahi; L G Beatty; P D Sadowski
Journal:  Nucleic Acids Res       Date:  1992-11-25       Impact factor: 16.971

2.  Domain of a yeast site-specific recombinase (Flp) that recognizes its target site.

Authors:  J W Chen; B R Evans; S H Yang; D B Teplow; M Jayaram
Journal:  Proc Natl Acad Sci U S A       Date:  1991-07-15       Impact factor: 11.205

3.  Protein-induced local DNA bends regulate global topology of recombination products.

Authors:  Quan Du; Alexei Livshits; Agnieszka Kwiatek; Makkuni Jayaram; Alexander Vologodskii
Journal:  J Mol Biol       Date:  2007-02-11       Impact factor: 5.469

4.  Synapsis, strand scission, and strand exchange induced by the FLP recombinase: analysis with half-FRT sites.

Authors:  A Amin; H Roca; K Luetke; P D Sadowski
Journal:  Mol Cell Biol       Date:  1991-09       Impact factor: 4.272

5.  Determinants of the position of a Flp-induced DNA bend.

Authors:  K H Luetke; P D Sadowski
Journal:  Nucleic Acids Res       Date:  1998-03-15       Impact factor: 16.971

6.  Asymmetry in Flp-mediated cleavage.

Authors:  K H Luetke; B P Zhao; P D Sadowski
Journal:  Nucleic Acids Res       Date:  1997-11-01       Impact factor: 16.971

7.  Selection of novel, specific single-stranded DNA sequences by Flp, a duplex-specific DNA binding protein.

Authors:  X D Zhu; P D Sadowski
Journal:  Nucleic Acids Res       Date:  1998-03-01       Impact factor: 16.971

8.  Mechanism of cleavage and ligation by FLP recombinase: classification of mutations in FLP protein by in vitro complementation analysis.

Authors:  G Pan; K Luetke; P D Sadowski
Journal:  Mol Cell Biol       Date:  1993-06       Impact factor: 4.272

9.  Mechanism of active site exclusion in a site-specific recombinase: role of the DNA substrate in conferring half-of-the-sites activity.

Authors:  J Lee; T Tonozuka; M Jayaram
Journal:  Genes Dev       Date:  1997-11-15       Impact factor: 11.361

10.  Chemical probe and missing nucleoside analysis of Flp recombinase bound to the recombination target sequence.

Authors:  A S Kimball; M L Kimball; M Jayaram; T D Tullius
Journal:  Nucleic Acids Res       Date:  1995-08-11       Impact factor: 16.971

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.