FLP1/R0010W Literature Guide Help

Other names published for FLP1: R0010W

FLP1 - Mutants/Phenotypes (19)

ReferenceOther Genes Addressed
Okamoto H, et al.  (2011) Double rolling circle replication (DRCR) is recombinogenic. Genes Cells 16(5):503-13
Xiong L, et al.  (2009) Deficient SUMO attachment to Flp recombinase leads to homologous recombination-dependent hyperamplification of the yeast 2 microm circle plasmid. Mol Biol Cell 20(4):1241-51
Viscardi V, et al.  (2007) MRX-dependent DNA damage response to short telomeres. Mol Biol Cell 18(8):3047-58
Whiteson KL, et al.  (2007) Identification of a potential general acid/base in the reversible phosphoryl transfer reactions catalyzed by tyrosine recombinases: Flp H305. Chem Biol 14(2):121-9
Voziyanov Y, et al.  (2003) Stepwise manipulation of DNA specificity in Flp recombinase: progressively adapting Flp to individual and combinatorial mutations in its target site. J Mol Biol 326(1):65-76
Grainge I, et al.  (2001) DNA recombination and RNA cleavage activities of the Flp protein: roles of two histidine residues in the orientation and activation of the nucleophile for strand cleavage. J Mol Biol 314(4):717-33
Tribble G, et al.  (2000) DNA recognition, strand selectivity, and cleavage mode during integrase family site-specific recombination. J Biol Chem 275(29):22255-67
Lee J, et al.  (1997) Mechanism of active site exclusion in a site-specific recombinase: role of the DNA substrate in conferring half-of-the-sites activity. Genes Dev 11(22):3061-71
Lee J and Jayaram M  (1995) Functional roles of individual recombinase monomers in strand breakage and strand union during site-specific DNA recombination. J Biol Chem 270(39):23203-11
Zhu XD and Sadowski PD  (1995) Cleavage-dependent ligation by the FLP recombinase. Characterization of a mutant FLP protein with an alteration in a catalytic amino acid. J Biol Chem 270(39):23044-54
Serre MC and Jayaram M  (1992) Half-site strand transfer by step-arrest mutants of yeast site-specific recombinase Flp. J Mol Biol 225(3):643-9
Chen JW, et al.  (1991) Tyr60 variants of Flp recombinase generate conformationally altered protein-DNA complexes. Differential activity in full-site and half-site recombinations. J Mol Biol 218(1):107-18
Schwartz CJ and Sadowski PD  (1990) FLP protein of 2 mu circle plasmid of yeast induces multiple bends in the FLP recognition target site. J Mol Biol 216(2):289-98
Amin AA and Sadowski PD  (1989) Synthesis of an enzymatically active FLP recombinase in vitro: search for a DNA-binding domain. Mol Cell Biol 9(5):1987-95
Schwartz CJ and Sadowski PD  (1989) FLP recombinase of the 2 microns circle plasmid of Saccharomyces cerevisiae bends its DNA target. Isolation of FLP mutants defective in DNA bending. J Mol Biol 205(4):647-58
Lebreton B, et al.  (1988) Mutations that improve the binding of yeast FLP recombinase to its substrate. Genetics 118(3):393-400
Govind NS and Jayaram M  (1987) Rapid localization and characterization of random mutations within the 2 micron circle site-specific recombinase: a general strategy for analysis of protein function. Gene 51(1):31-41
Reynolds AE, et al.  (1987) Roles of the 2 microns gene products in stable maintenance of the 2 microns plasmid of Saccharomyces cerevisiae. Mol Cell Biol 7(10):3566-73
Broach JR, et al.  (1982) Recombination within the yeast plasmid 2mu circle is site-specific. Cell 29(1):227-34