Processing of recombination intermediates by the RecG and RuvAB proteins of Escherichia coli.
AuthorsLloyd RG, Sharples GJ
JournalNucleic Acids Res
PubMed ID8388095
The RuvAB, RuvC and RecG proteins of Escherichia coli process intermediates in recombination and DNA repair into mature products. RuvAB and RecG catalyse branch migration of Holliday junctions, while RuvC resolves these structures by nuclease cleavage around the point of strand exchange. The overlap between RuvAB and RecG was investigated ... More
An entire functional mammary gland may comprise the progeny from a single cell.
AuthorsKordon EC, Smith GH
JournalDevelopment
PubMed ID9550724
'Any epithelial portion of a normal mouse mammary gland can reproduce an entire functional gland when transplanted into an epithelium-free mammary fat pad. Mouse mammary hyperplasias and tumors are clonal dominant populations and probably represent the progeny of a single transformed cell. Our study provides evidence that single multipotent stem ... More
Localization of cholinergic differentiation factor/leukemia inhibitory factor mRNA in the rat brain and peripheral tissues.
AuthorsYamamori T
JournalProc Natl Acad Sci U S A
PubMed ID1714598
'Sympathetic neurons display considerable plasticity in the neurotransmitter and neuropeptide phenotypes they express in vitro and in vivo. The cholinergic differentiation factor (CDF, also known as leukemia inhibitory factor, LIF) induces cultured rat sympathetic neurons to become cholinergic, without affecting their survival or growth. To understand the role of this ... More
A mutation in helicase motif III of E. coli RecG protein abolishes branch migration of Holliday junctions.
AuthorsSharples GJ, Whitby MC, Ryder L, Lloyd RG
JournalNucleic Acids Res
PubMed ID8127666
'The RecG protein of Escherichia coli catalyses branch migration of Holliday junctions made by RecA and dissociates synthetic X junctions into duplex products in reactions that require hydrolysis of ATP. To investigate the mode of action of this enzyme a chromosomal mutation that inactivates recG (recG162) was cloned and sequenced. ... More
Resolution of Holliday junctions by RuvC resolvase: cleavage specificity and DNA distortion.
AuthorsBennett RJ, Dunderdale HJ, West SC
JournalCell
PubMed ID8402879
E. coli RuvC protein resolves Holliday junctions during genetic recombination and postreplication repair. Using small synthetic junctions, we show that junction recognition is structure-specific and occurs in the absence of metal cofactors. In the presence of Mg2+, Holliday junctions are resolved by the introduction of symmetrically related nicks at the ... More
An E. coli RuvC mutant defective in cleavage of synthetic Holliday junctions.
AuthorsSharples GJ, Lloyd RG
JournalNucleic Acids Res
PubMed ID8393986
Escherichia coli RuvC protein is a specific endonuclease that resolves recombination intermediates into viable products. The structural features needed for RuvC activity were investigated by sequencing three ruvC mutations and relating the base pair changes identified to the activity of the mutant proteins. Each of the three mutations is a ... More
Molecular and immunological characterization of ADP-ribosylarginine hydrolases.
Mono-ADP-ribosylation is a reversible modification of proteins with NAD:arginine ADP-ribosyltransferases and ADP-ribosylarginine hydrolases catalyzing the forward and reverse reactions, respectively. Hydrolase activities were present in a variety of animal species, with the highest specific activities found in rat and mouse brain, spleen, and testis. Rat and mouse hydrolases were dithiothreitol- ... More