Interaction between domains in chromosomal protein HMG-1.

Carballo, Miguel; Puigdomènech, Pere; Tancredi, Teodorico; Palau, Jaume

doi:10.1002/j.1460-2075.1984.tb01960.x

Cited by 49 publications

(32 citation statements)

References 31 publications

(37 reference statements)

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“…8B). Even though V1 contains domain B, it has been shown to be quite different from V2 alone, having very little secondary structure as measured by spectroscopic techniques (Carballo et al 1984). This effect has been ascribed to destabilizing effects of the acidic tail on domain B when separated from domain A. V1, like V3, was not active in DNA bending (Fig.…”

Section: Domain B Of Hmg1 Is Sufficient For Bending Activitymentioning

confidence: 99%

“…Protease digestion experiments, secondary structure predictions, and DNA-binding studies indicate that HMG1 and HMG2 have three major structural domains (Reeck 1982;Carballo et al 1983Carballo et al , 1984Bianchi et al 1992). The DNA-binding portions of the proteins are composed of two relatively basic regions, termed domains A and B, which are -47% similar but only 27% identical to each other in amino acid sequence.…”

Section: Domain B Of Hmg1 Is Sufficient For Bending Activitymentioning

confidence: 99%

“…As diagramed in Figure 7, when HMG1 or HMG2 is incubated with low concentrations of V8 protease for a short time, intact protein fragments can be recovered that correspond roughly to the structural domains. Isolated V3 (approximately domain A} and V2 (approximately domain B) have high R-helical content and bind duplex DNA, whereas V1 (approximately domain B plus acidic tail) is comparatively unstructured and does not bind DNA (Carballo et al 1983(Carballo et al , 1984. Figure 8A shows the results of inversion assays with isolated V2 and V3 peptides.…”

Section: Domain B Of Hmg1 Is Sufficient For Bending Activitymentioning

confidence: 99%

“…7): the amino-terminal and central regions (domains A and B), which have internal homology and can bind DNA independently (Carballo et al 1983(Carballo et al , 1984Bianchi et al 1992), and the carboxy-terminal acidic tail, which can interact with histone H1 in vitro (Carballo et al 1983}. HMG3, a degradation product of HMG1 missing the acidic tail, is active in promoting invertasome assembly as well as DNA bending, demonstrating that the carboxy-terminal region is not required for these functions.…”

Section: Activities Of Isolated Polypeptides From Hmg1mentioning

confidence: 99%

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The nonspecific DNA-binding and -bending proteins HMG1 and HMG2 promote the assembly of complex nucleoprotein structures.

1993

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The mammalian high mobility group proteins HMG1 and HMG2 are abundant, chromatin-associated proteins whose cellular function is not known. In this study we show that these proteins can substitute for the prokaryotic DNA-bending protein HU in promoting the assembly of the Hin invertasome, an intermediate structure in Hin-mediated site-specific DNA inversion. Formation of this complex requires the assembly of the Hin recombinase, the Fis protein, and three cis-acting DNA sites, necessitating the looping of intervening DNA segments. Invertasome assembly is strongly stimulated by HU or HMG proteins when one of these segments is shorter than 104 bp. By use of ligase-mediated circularization assays, we demonstrate that HMG1 and HMG2 can bend DNA extremely efficiently, forming circles as small as 66 bp, and even 59-bp circles at high HMG protein concentrations. In both invertasome assembly and circularization assays, substrates active in the presence of HMG1 contain one less helical turn of DNA compared with substrates active in the presence of HU protein. Analysis of different domains of HMG1 generated by partial proteolytic digestion indicate that DNA-binding domain B is sufficient for both bending and invertasome assembly. We suggest that an important biological function of HMG1 and HMG2 is to facilitate cooperative interactions between cis-acting proteins by promoting DNA flexibility. A general role for HMG1 and HMG2 in chromatin structure is also suggested by their ability to wrap DNA duplexes into highly compact forms.

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Section: Domain B Of Hmg1 Is Sufficient For Bending Activitymentioning

confidence: 99%

Section: Domain B Of Hmg1 Is Sufficient For Bending Activitymentioning

confidence: 99%

Section: Domain B Of Hmg1 Is Sufficient For Bending Activitymentioning

confidence: 99%

Section: Activities Of Isolated Polypeptides From Hmg1mentioning

confidence: 99%

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The nonspecific DNA-binding and -bending proteins HMG1 and HMG2 promote the assembly of complex nucleoprotein structures.

1993

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“…studies have shown that binding of HMG1 to DNA is influenced by the highly charged COOH-terminal domain of the molecule (14,15,43,44). We wished to analyze the effect of this region on the interaction of HMG1 with the irradiated oligonucleotides.…”

Section: Binding Of Hmg1 Protein Lacking the Acidic Carboxyl-terminalmentioning

confidence: 99%

Preferential Binding of High Mobility Group 1 Protein to UV-damaged DNA

Pasheva¹,

Pashev²,

Favre³

1998

Journal of Biological Chemistry

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Binding of chromosomal high mobility group 1 protein (HMG1) to UV-damaged DNA has been studied with oligonucleotides containing a single dipyrimidine site for formation of UV photolesions. Irradiation of an oligonucleotide with unique TT dinucleotide resulted in generation of cyclobutane pyrimidine dimer with no evidence for induction of (6-4) photoproducts, whereas the analysis of irradiated TC-containing oligonucleotide detected (6-4) photoproducts but not cyclobutane pyrimidine dimers. Mobility shift assays have revealed that HMG1 protein binds preferentially to irradiated TT and TC oligonucleotides. Photoreversal of cyclobutane pyrimidine dimers with DNA photolyase and hydrolysis of the (6-4) photoproducts with hot alkali substantially reduced but did not eliminate binding of HMG1. The protein, therefore, appears to bind the two main types of UV damages in DNA, but some other photolesion(s) contributes to the preferential binding of HMG1 to irradiated DNA. By quantifying gel shift assays and considering the efficiencies of lesion formation, we determined dissociation constants of 1.2 ؎ 0.5 and 4.0 ؎ 1.5 M for irradiated TT and TC oligonucleotides, respectively, and 70 ؎ 20 M for the control non-irradiated probes. Tryptic removal of the acidic COOH-terminal domain of HMG1 significantly affected binding of the protein to both irradiated and intact oligonucleotides. The potential role of HMG1 in recognition of the UV lesions in DNA is discussed.High mobility group proteins 1 and 2 (HMG1 and -2) 1 are abundant chromosomal proteins found in a variety of eukaryotic species. Despite their early identification and biochemical characterization (1) and subsequent implication in a number of cellular events, their functions are still unknown (for reviews see Refs. 2 and 3). The interest in these proteins sharply increased in the early 1990s with the discovery of a new kind of eukaryotic protein domain involved in interactions with DNA (4), which displayed sequence similarity to two homologous repeats of an 80-amino acid sequence in HMG1. This motif called HMG box was found in a wealth of less abundant eukaryotic proteins, mainly general transcription factors and gene-specific transcriptional activators (reviewed in Refs. 3 and 5). A general characteristic of these proteins is their ability to bind bent DNA or to induce bending in DNA independent of sequence or the existence of prebent regions (6). Thus, HMG1 binds preferentially to distorted DNA sites such as synthetic cruciform DNA structures (7,8) and the lesions formed on DNA by the anticancer drug cisplatin (9, 10). The ability of HMG box-containing proteins to mediate bending in linear duplex DNA was demonstrated by several approaches (11-13). In addition, these proteins can constrain negative supercoils in plasmid DNA (14 -16) and can serve as "architectural" elements in the assembly of higher order nucleoprotein complexes (5,11,13,(17)(18)(19).The finding that HMG1 binds more tightly to cisplatin-damaged DNA than to unmodified B form DNA implies that the signal f...

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Protein chemistry‐nuclear magnetic resonance approach to mapping functional domains in single‐stranded DNA binding proteins

Coleman

Williams

King

et al. 1986

J of Cellular Biochemistry

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DNA binding proteins that bind preferentially to single-stranded DNA with relatively little sequence specificity are widely distributed in both prokaryotic and eukaryotic cells. These proteins function in DNA replication and recombination and are synthesized in high enough copy number to suggest that they act in vivo by forming stoichiometric complexes with exposed single-stranded regions of DNA. Some proteins of this class also have significant affinity for single-stranded RNA and may thus influence translation as well. The single-stranded DNA binding proteins coded for by gene 32 of bacteriophage T4 and by gene 5 of the filamentous bacteriophage fd (M13) are the most extensively investigated examples of this class of proteins. The location of the DNA binding domains in the primary structure, the thermodynamics of DNA binding and the specific amino acid residues responsible for the nucleotide-protein interactions have been successfully determined for these proteins by a variety of physicochemical techniques, which include limited proteolysis to determine minimum DNA binding domains, chemical modification to detect specific types of amino acid side chain involved in DNA binding, and a number of one-and two-dimensional 'H-nuclear magnetic resonance (NMR) techniques to detect proteinoligonucleotide interactions. A crystal structure is available for the unliganded gene 5 protein, facilitating the detailed study of these interactions. Recently, a program of site-directed mutagenesis has been untertaken to detect specific residues participating in DNA binding and to assign the 'H-NMR spectra residue by residue. Examples of the information obtained by these methods and the synthesis of the findings into models for the binding of single-stranded DNA by these proteins are covered in this review.

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Interaction between domains in chromosomal protein HMG-1.

Cited by 49 publications

References 31 publications

The nonspecific DNA-binding and -bending proteins HMG1 and HMG2 promote the assembly of complex nucleoprotein structures.

The nonspecific DNA-binding and -bending proteins HMG1 and HMG2 promote the assembly of complex nucleoprotein structures.

Preferential Binding of High Mobility Group 1 Protein to UV-damaged DNA

Protein chemistry‐nuclear magnetic resonance approach to mapping functional domains in single‐stranded DNA binding proteins

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