Leucine-induced Dissociation of Escherichia coli Lrp Hexadecamers to Octamers

Chen, Shaolin; Calvo, Joseph M.

doi:10.1016/s0022-2836(02)00187-0

Cited by 80 publications

(112 citation statements)

References 21 publications

Supporting

Mentioning

102

Contrasting

Unclassified

Order By: Relevance

“…This appears to occur as a result of diminished PapI homologue-dependent binding of Lrp to GATC dist and increased binding of Lrp to GATC prox , locking cells in the OFFphase transcription state. Lrp has a binding site for aliphatic amino acids, which appears to modulate the multimeric state of Lrp between dimeric, octameric, and hexadecameric states (57,59). If Lrp binding sites are phased such that they occur on the same DNA face, then an octameric Lrp could engage up to four sites, contributing to binding cooperativity.…”

Section: Pap-related Systemsmentioning

confidence: 99%

Epigenetic Gene Regulation in the Bacterial World

Casadesús

Low

2006

Microbiol Mol Biol Rev

567

562

View full text Add to dashboard Cite

SUMMARY Like many eukaryotes, bacteria make widespread use of postreplicative DNA methylation for the epigenetic control of DNA-protein interactions. Unlike eukaryotes, however, bacteria use DNA adenine methylation (rather than DNA cytosine methylation) as an epigenetic signal. DNA adenine methylation plays roles in the virulence of diverse pathogens of humans and livestock animals, including pathogenic Escherichia coli, Salmonella, Vibrio, Yersinia, Haemophilus, and Brucella. In Alphaproteobacteria, methylation of adenine at GANTC sites by the CcrM methylase regulates the cell cycle and couples gene transcription to DNA replication. In Gammaproteobacteria, adenine methylation at GATC sites by the Dam methylase provides signals for DNA replication, chromosome segregation, mismatch repair, packaging of bacteriophage genomes, transposase activity, and regulation of gene expression. Transcriptional repression by Dam methylation appears to be more common than transcriptional activation. Certain promoters are active only during the hemimethylation interval that follows DNA replication; repression is restored when the newly synthesized DNA strand is methylated. In the E. coli genome, however, methylation of specific GATC sites can be blocked by cognate DNA binding proteins. Blockage of GATC methylation beyond cell division permits transmission of DNA methylation patterns to daughter cells and can give rise to distinct epigenetic states, each propagated by a positive feedback loop. Switching between alternative DNA methylation patterns can split clonal bacterial populations into epigenetic lineages in a manner reminiscent of eukaryotic cell differentiation. Inheritance of self-propagating DNA methylation patterns governs phase variation in the E. coli pap operon, the agn43 gene, and other loci encoding virulence-related cell surface functions.

show abstract

Section: Pap-related Systemsmentioning

confidence: 99%

Epigenetic Gene Regulation in the Bacterial World

Casadesús

Low

2006

Microbiol Mol Biol Rev

567

562

View full text Add to dashboard Cite

show abstract

“…In the presence of leucine, Lrp changes its association state from hexadecamers to octamers. 22) In the presence of lysine, FL11 assembles to octamers. 7,9) Arginine facilitates hetero-octamerization by two FL11 dimers and two DM1 dimers.…”

Section: D Structure and Molecular Recognitionmentioning

confidence: 99%

“…4C). All the FFRPs known to interact with amino acids have Asp at position 104 and Thr or Ser at one of 133-135: in eubacteria Lrp interacts with leucine 22,26) ; PutR interacts with proline 27) ; BkdR interacts with valine, isoleucine and leucine 28) ; NMB 0572 interacts with leucine and methionine 10) ; MdeR potentially interacts with methionine 29) ; and Grp potentially interacts with glutamic acid 30) : in archaea LysM interacts with lysine 31) ; TvFL3 (tvg1179749) also interacts with lysine 9) ; DM2 (pot0300646) and FL9 (pot0301583) interact with glutamine 9) ; DM3 (pot0175330), TvDM (tvg0307586) and FL5 (pot1664679) interact with hydrophobic amino acids 9) ; FL4 (pot1613368) interacts with glutamic acid. 9) Thus an FFRP having Asp104 and Thr/Ser at one of the positions 133-135 is predicted to interact with a ligand amino acid.…”

Section: D Structure and Molecular Recognitionmentioning

confidence: 99%

“…22) This change might affect binding of Lrp to promoters: to a promoter having more than four dimer-binding sites, binding is expected to be tighter in the absence of leucine. Alternatively, interaction with leucine might cover or uncover a surface used for interaction with other transcription factors.…”

Section: ) Similarities Between Regulations By Eubac-terial Lrp Andmentioning

confidence: 99%

See 1 more Smart Citation

Transcription Regulation by Feast/Famine Regulatory Proteins, FFRPs, in Archaea and Eubacteria

Kawashima

Aramaki

Oyamada

et al. 2008

Biological & Pharmaceutical Bulletin

View full text Add to dashboard Cite

“…four pairs of dimers), either binding or not binding DNA 2) : here referred to as tetrameric assemblies. In fact, the tetrameric assembly form is most common among FFRPs in crystal as well as in solution: E. coli LRP, 15) LrpA, 16) and pot1216151 (DM1). 13), 14) In short, FL11 has multiple assembly forms, and the aim of this paper is to further characterize particles (i.e.…”

Section: )mentioning

confidence: 99%

An electron microscopic study of the archaeal feast/famine regulatory protein

Ishijima

Clowney

Suzuki

2004

Proceedings of the Japan Academy. Ser. B: Physical and Biologic

View full text Add to dashboard Cite

Abstract:Particles formed by a feast/famine regulatory protein (FFRP), pot0434017 (FL11), in solution in the absence of DNA were analyzed using electron microscopy (EM). By applying conventional (i.e. dry) EM to the protein negatively stained with uranyl acetate, top views of tetrameric assemblies of dimers were obtained, where four pairs each of N-domains were extending from C-domains assembled around the centers. In cryo-EM images of the protein embedded in 3D amorphous ice, sets of four densities were arranged around ellipsoids having similar lengths for their long axes but of different lengths for their short axes. These images were interpreted as projections with different tilts of four pairs of N-domains arranged inside flat assemblies: the positively charged N-domains only were stained with ammonium molybdate, but the negatively charged C-domains were unstained and thus unobservable. Using seventeen such cryo-images, in combination with a crystal structure equivalent to an assembly of C-domains, a disk-like 3D structure was reconstructed.

show abstract

Leucine-induced Dissociation of Escherichia coli Lrp Hexadecamers to Octamers

Cited by 80 publications

References 21 publications

Epigenetic Gene Regulation in the Bacterial World

Epigenetic Gene Regulation in the Bacterial World

Transcription Regulation by Feast/Famine Regulatory Proteins, FFRPs, in Archaea and Eubacteria

An electron microscopic study of the archaeal feast/famine regulatory protein

Contact Info

Product

Resources

About