‘SPKK’ motifs prefer to bind to DNA at A/T-rich sites.

Churchill, Mair E. A.; Suzuki, Masashi

doi:10.1002/j.1460-2075.1989.tb08604.x

Cited by 186 publications

(103 citation statements)

References 61 publications

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“…Amino acid motifs such as SPKK, which was originally found in histone HI, and subsequently in several other DNA-binding proteins (Suzuki, 1989), may provide this specificity for SAR binding. The dimer (SPKK)^ binds preferentially to the minor groove of AT-rich DNA (Churchill and Suzuki, 1989).…”

Section: Proteins That Bind Sarsmentioning

confidence: 99%

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DNA loops: structural and functional properties of scaffold‐attached regions

Roberge

Gasser²

1992

Molecular Microbiology

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SummaryThe long DNA molecules of eukaryotic genomes appear to be organized into large loops formed by the binding of dispersed DNA sequences to non-histone proteins. This partitioning of DNA into topologically constrained units constitutes one of the highest orders of DNA packing in chromosomes. DNA loops are likely to define functional units as well as topologjcal domains, contributing to the regulation of gene expression and DNA replication. This review presents recent work on the properties of the DNA sequences and proteins thought to be involved in loop formation, and on their possible significance for replication and transcription.The nuclear and chromosomal scaffoldThe nuclear and chromosomal scaffolds are operationally defined structures that can be isolated from interphase nuclei and metaphase chromosomes of eukaryotic cells (Cook and Brazell, 1975; Paulson and Laemmli, 1977). In brief, scaffolds are the structures that remain after the removal of histones and soluble proteins with low concentrations of a detergent-like chaotrope, lithium-3',5'-diiodosalicylate (Mirkovitch et al., 1984). Previously 2M NaCI had been used to produce substructures similar in many respects. The scaffolds maintain site-specific interaction with genomic DNA, restraining the genome topologically and apparently defining the bases of DNA loops. The ability of the scaffold to resist solubilization in vitro depends in part on the presence of heavy metals (especially Cu^"") or on a brief exposure to 37°C in vitro.The protein composition of the nuclear scaffold is complex. It includes the nuclear lamins and pore proteins at the nuclear periphery, as well as an ill-defined internal

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Section: Proteins That Bind Sarsmentioning

confidence: 99%

“…The dimer (SPKK)^ binds preferentially to the minor groove of AT-rich DNA (Churchill and Suzuki, 1989). like Histone HI and topoisomerase II do, although other motifs with similar DNA-binding properties have also been described (Reeves and Nissen.…”

Section: Proteins That Bind Sarsmentioning

confidence: 99%

DNA loops: structural and functional properties of scaffold‐attached regions

Roberge

Gasser²

1992

Molecular Microbiology

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“…It has been proposed that the histone Hl-DNA interaction implicates the DNA-binding peptide motif SPXX (X for a basic residue) [6,7]. Analogous basic peptides have been shown to be implicated in sequence-specific histone-DNA recognition processes [8,9]. Clustered S(T)-P-X-Basic motifs promote DNA-histone interactions [lo] and their phosphorylation [12,13] or acetylation [14] appear as many regulatory processes involved in chromatin condensation.…”

Section: Introductionmentioning

confidence: 99%

“…poly(dA-dT). The octapeptide SPRKSPRK is found at the amino and carboxyl termini of histone Hl and the amino terminus of H2B from sea urchin sperm and binds selectively to AT-rich DNA sequences [6,8,15] …”

Section: Introductionmentioning

confidence: 99%

“…pH 6 5 were scanned usmg l-cm pathlength quartz cuvettes Measurements were made by progressrve additton of the pepttde to a pure DNA (or polynucleotide) solutton at 100 PM to get the desired ligand/phosphate-DNA (L/P) ratto. The molar elhpttctty [8] was expressed in deg cm' dmol-' per nucleottde. The CD spectra of the different homopolymers and alternating copolymers recorded under low ionic condtttons (1 mM sodmm tons) are m agreement with those reported m [20] obtamed at a htgher iomc strength (1 mM phosphate buffer contammg IO mM NaCl).…”

Section: Introductionmentioning

confidence: 99%

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A tandem repeat of the SPKK peptide motif induces Ψ‐type DNA structures at alternating AT sequences

Bailly

Colson

et al. 1993

FEBS Letters

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The interaction between a tandem repeat of the SPKK peptlde motif and calf thymus DNA or several polynucleotides has been investigated by circular dlchroism.The octapeptide SPKKSPKK does not Induce any Important changes in the CD spectra of the polynucleotldes poly(dG) poly(dC), poly(dG-dC) poly(dG-dC) and poly(dA) poly(dT) whde the spectrum of calf thymus DNA is slightly modified. Binding of this basic peptide to the alternating copolymer poly(dA-dT) poly(dA-dT) results m a marked Y-type condensation in a manner similar to that induced by the entire C-termmal domain of histone Hl.

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Carboxyl-terminal peptides from histone H1 variants: DNA binding characteristics and solution conformation

Wellman¹

1998

Biopolymers

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The carboxyl‐terminal domains of the histone H1 proteins bind to DNA and are important in condensation of DNA. Little is known about the details of the interactions between H1 histones and DNA, and in particular, there is little known about differences among variant H1 histones in their interactions with DNA. Questions concerning H1 histone‐DNA affinity and H1 conformation were investigated using peptide fragments from the carboxyl terminal domains of four nonallelic histone H1 variant proteins (mouse H1‐1, H1‐4 and H1°, and rat H1T). Three of the four peptides showed a slight preference for binding to a GC‐rich region of a 214‐base‐pair DNA fragment, rather than to an AT‐rich region. The fourth peptide, H1t, appeared to bind preferentially to the AT‐rich region of the 214‐base‐pair fragment. The results show that these small peptides bind preferentially to a subset of DNA sequences; such sequence preference might be exhibited by the intact H1 histones themselves. CD spectra of the peptides, which are from regions of the proteins that are not compactly folded, showed that the α‐helical content of the peptides was minimal if the peptides were in 10 mM phosphate buffer, but increased if the peptides were in 1 M NaClO4 and 50% trifluoroethanol, conditions that are postulated to approximate certain aspects of binding to DNA. H1‐4 peptide, which was predicted to be 70% α‐helix, but was not α‐helical in 10 mM phosphate buffer, appeared from difference CD spectra to be more α‐helical when it was bound to DNA. The regions of the proteins from which these peptides are derived, which are extended in solution, may fold, forming α‐helices, upon binding to DNA. © 1996 John Wiley & Sons, Inc.

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‘SPKK’ motifs prefer to bind to DNA at A/T-rich sites.

Cited by 186 publications

References 61 publications

DNA loops: structural and functional properties of scaffold‐attached regions

DNA loops: structural and functional properties of scaffold‐attached regions

A tandem repeat of the SPKK peptide motif induces Ψ‐type DNA structures at alternating AT sequences

Carboxyl-terminal peptides from histone H1 variants: DNA binding characteristics and solution conformation

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