Membrane regulation of the chromosomal replication activity of E. coli DnaA requires a discrete site on the protein.

Garner, Jennifer; Crooke, E.

doi:10.1002/j.1460-2075.1996.tb00714.x

Cited by 82 publications

(97 citation statements)

References 14 publications

(16 reference statements)

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“…Such features are described for many proteins binding to lipid bilayer surfaces, and they are analyzed in more detail for a number of established amphipathic helices from the latter (recently reviewed by Johnson and Cornell (52)). Most similar in this collection of amphipathic helices was a membrane binding segment of DnaA (positions 366 -388), initiating chromosome replication in E. coli (53); it aligned with positions 218 -240 in the region with the largest hydrophobic moment of the entire alMGS sequence (cf. Figs.…”

Section: Discussionmentioning

confidence: 99%

Sequence Properties of the 1,2-Diacylglycerol 3-Glucosyltransferase from Acholeplasma laidlawiiMembranes

Berg

Edman

et al. 2001

Journal of Biological Chemistry

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Synthesis of the nonbilayer-prone ␣-monoglucosyldiacylglycerol (MGlcDAG) is crucial for bilayer packing properties and the lipid surface charge density in the membrane of Acholeplasma laidlawii. The gene for the responsible, membrane-bound glucosyltransferase (alMGS) (EC 2.4.1.157) was sequenced and functionally cloned in Escherichia coli, yielding MGlcDAG in the recombinants. Similar amino acid sequences were encoded in the genomes of several Gram-positive bacteria (especially pathogens), thermophiles, archaea, and a few eukaryotes. All of these contained the typical EX 7 E catalytic motif of the CAZy family 4 of ␣-glycosyltransferases. The synthesis of MGlcDAG by a close sequence analog from Streptococcus pneumoniae (spMGS) was verified by polymerase chain reaction cloning, corroborating a connection between sequence and functional similarity for these proteins. However, alMGS and spMGS varied in dependence on anionic phospholipid activators phosphatidylglycerol and cardiolipin, suggesting certain regulatory differences. Fold predictions strongly indicated a similarity for alMGS (and spMGS) with the two-domain structure of the E. coli MurG cell envelope glycosyltransferase and several amphipathic membrane-binding segments in various proteins. On the basis of this structure, the alMGS sequence charge distribution, and anionic phospholipid dependence, a model for the bilayer surface binding and activity is proposed for this regulatory enzyme.Lipids are the local environment for most integral and peripheral membrane proteins, which often depend on the lipids for optimal function. The large diversity of lipids and the differences in composition and properties between membranes have made it difficult to find out common features of bilayer organization and how lipids and proteins are cooperating in local processes. Lipid-synthesizing pathways have been mapped for the most common types of lipids, and several of the corresponding enzymes catalyzing these reactions have been characterized. However, when it comes to the connection between regulation of bilayer properties and enzyme structure, very little is known (1). So far, only a few lipid-synthesizing enzymes have been crystallized. Which structural properties are involved in the catalytic mechanism of these lipid enzymes, and how are the membrane properties sensed (1)?In the well characterized plasma membrane of Acholeplasma laidlawii, the lipid composition is regulated in a manner to maintain (i) lipid phase equilibria, close to a potential bilayer to nonbilayer transition, (ii) a nearly constant radius of spontaneous curvature, and (iii) a certain anionic surface charge density of the lipid bilayer. The synthesis of the major nonbilayer-prone lipid in this membrane, monoglucosyldiacylglycerol (MGlcDAG) 1 (Scheme 1, step I), plays an important role to fulfill the two first points above but also the third, since it is strongly regulated by negatively charged lipids (e.g. the major in vivo lipid phosphatidylglycerol (PG)) (2). MGlcDAG is consecutively processed into...

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Section: Discussionmentioning

confidence: 99%

Sequence Properties of the 1,2-Diacylglycerol 3-Glucosyltransferase from Acholeplasma laidlawiiMembranes

Berg

Edman

et al. 2001

Journal of Biological Chemistry

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“…DnaA is made up of 467 amino acid residues and has several functional domains (Sutton and Kaguni, 1997;Messer, 2002). Those domains of DnaA are involved in the binding of this protein to DNA (Roth and Messer, 1995), RepA protein (Sutton and Kaguni, 1995), ATP , DnaB (Marszalek et al, 1996), acidic membrane (Garner and Crooke, 1996) and in its self-oligomerization (Weigel et al, 1999). These domains are present in the above order from C to N termini of the DnaA protein (see Fig.…”

Section: Figmentioning

confidence: 99%

The Bacteriophage λ DNA Replication Protein P Inhibits the oriC DNA- and ATP-binding Functions of the DNA Replication Initiator Protein DnaA of Escherichia coli

Sau¹,

Sil²,

Mandal³

2005

BMB Reports

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Under the condition of expression of λ P protein at lethal level, the oriC DNA-binding activity is significantly affected in wild-type E. coli but not in the rpl mutant. In purified system, the λ P protein inhibits the binding of both oriC DNA and ATP to the wild-type DnaA protein but not to the rpl DnaA protein. We conclude that the λ P protein inhibits the binding of oriC DNA and ATP to the wild-type DnaA protein, which causes the inhibition of host DNA synthesis initiation that ultimately leads to bacterial death. A possible beneficial effect of this interaction of λ P protein with E. coli DNA initiator protein DnaA for phage DNA replication has been proposed.

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“…The PEND protein is, in contrast, an integral membrane protein of the inner envelope membrane and is only solubilized with a high concentration of detergent (see Results). Bacterial DNA binding proteins, such as SeqA and DnaA, that are known to bind to the membrane may not be integral membrane proteins because they are purified as soluble proteins (Slater et al, 1995;Garner and Crooke, 1996).…”

Section: Molecular Features and Dna Binding Of The Pend Proteinmentioning

confidence: 99%

Molecular Characterization of the PEND Protein, a Novel bZIP Protein Present in the Envelope Membrane That Is the Site of Nucleoid Replication in Developing Plastids

Sato

Ohshima²,

Watanabe

et al. 1998

Plant Cell

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Plastid nucleoids are known to bind to the envelope membrane in developing chloroplasts. Here, plastid DNA is extensively replicated. We previously detected a DNA binding protein in the inner envelope membranes of developing plastids in pea and named it PEND (for plastid envelope DNA binding) protein. In this study, we report on the structure and molecular characterization of a cDNA for the PEND protein. As a result of screening cDNA libraries in gt11 with one of the target sequences of the PEND protein as a probe, we obtained a clone (PD2) for a novel DNA binding protein consisting of 633 amino acid residues. Analysis of the N-terminal sequence of the purified PEND protein indicated that the transit peptide is just 16 residues long. The PEND protein was detected specifically in the plastid envelope membrane of young unopened leaf buds by immunoblot analysis. The PEND protein consists of a basic region plus zipper region, an unprecedented sextuple repeat region, and a putative membrane-spanning region. The basic region with a zipper region seems to have diverged from that of other plant transcription factors. In addition, the PEND protein could be a distant homolog of the trans -Golgi network integral membrane proteins. The PEND protein is therefore a novel type of DNA binding protein that binds to the membrane as an intrinsic membrane protein.

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Membrane regulation of the chromosomal replication activity of E. coli DnaA requires a discrete site on the protein.

Cited by 82 publications

References 14 publications

Sequence Properties of the 1,2-Diacylglycerol 3-Glucosyltransferase from Acholeplasma laidlawiiMembranes

Sequence Properties of the 1,2-Diacylglycerol 3-Glucosyltransferase from Acholeplasma laidlawiiMembranes

The Bacteriophage λ DNA Replication Protein P Inhibits the oriC DNA- and ATP-binding Functions of the DNA Replication Initiator Protein DnaA of Escherichia coli

Molecular Characterization of the PEND Protein, a Novel bZIP Protein Present in the Envelope Membrane That Is the Site of Nucleoid Replication in Developing Plastids

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