HMG 14/17 binding affinities and DNAase I sensitivities of nucleoprotein particles

Stein, Arnold; Townsend, T. Matthew

doi:10.1093/nar/11.19.6803

Cited by 30 publications

(9 citation statements)

References 28 publications

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“…A number of observations indicate that HMG proteins have a structural role in chromatin. They are relatively abundant (_ 106 copies per nuclei, Goodwin et al, 1978a) and some of these fractions, HMG-14 and -17, have conformational effects on nucleosomes; these may be related to the DNase I sensitivity of specific zones of chromatin (Weisbrod et al, 1980;Stein and Townsend, 1983). In the case of HMG-1 and -2 less defined hypotheses have been proposed.…”

Section: Discussionmentioning

confidence: 99%

Interaction between domains in chromosomal protein HMG-1.

Carballo¹,

Puigdomènech²,

Tancredi³

et al. 1984

The EMBO Journal

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Peptides corresponding to the N‐terminal, central and central plus C‐terminal domains of high mobility group protein HMG‐1 from calf thymus have been isolated after digestion in solution with protease V8 under structuring conditions (0.35 M NaCl, pH 7.1). The effect of the interaction of these peptides with DNA on the topological properties of the nucleic acid has been studied and compared with the change in superhelicity produced by the whole protein. It appears that the region responsible for this effect is the central domain of HMG‐1. The isolated N‐terminal and central domains of this protein maintain their secondary and tertiary structure as observed by spectroscopic techniques. However, when the central domain is covalently linked only to the acidic C‐terminal part of the molecule, its secondary and tertiary structures are lost as well as its property to alter DNA superhelicity. The results are discussed in relation to the interactions occurring between the different domains and the possible functional interactions of this protein.

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Section: Discussionmentioning

confidence: 99%

Interaction between domains in chromosomal protein HMG-1.

Carballo¹,

Puigdomènech²,

Tancredi³

et al. 1984

The EMBO Journal

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“…It has been reported that the increased sensitivity of active chromatin domains to DNase I correlates with the presence of HMG-14 and/or HMG-17 (7,27). However, whether HMG-17 and HMG-14 are directly responsible for the increased DNase I-sensitivity is controversial (28)(29)(30)(31)(32). As an immature B-cell, DT40 expresses large amounts of immunoglobulin light-chain proteins from the rearranged copy of its λ light-chain gene.…”

Section: Lack Of Null-mutation Effects On Dnasei-hypersensitive Sitesmentioning

confidence: 99%

Neither HMG-14a nor HMG-17 gene function is required for growth of chicken DT40 cells or maintenance of DNaseI-hypersensitive sites

Strahler

Dodgson

1997

Nucleic Acids Research

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HMG-14 and HMG-17 form a family of ubiquitous non-histone chromosomal proteins and have been reported to bind preferentially to regions of active chromatin structure. Our previous studies demonstrated that the chicken HMG-17 gene is dispensable for normal growth of the DT40 chicken lymphoid cell line. Here it is shown that the major chicken HMG-14 gene,HMG-14a, is also dispensable and, moreover, that DT40-derived cells lacking both HMG-17 and HMG-14a proteins show no obvious change in phenotype with respect to the parental DT40 cells. Furthermore, no compensatory changes in HMG-14b or histone protein levels were observed in cells lacking both HMG-14a and HMG-17, nor were any alterations detected in such hallmarks of chromatin structure as DNaseI-hypersensitive sites or micrococcal nuclease digestion patterns. It is concluded that the HMG-14a and HMG-17 proteins are not required for normal growth of avian cell linesin vitro, nor for the maintenance of DNaseI-hypersensitive sites in chromatin.

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“…However, the subject is a matter of controversy (see e.g. Nicolas et al, 1983;Seale et al, 1983;Stein and Townsend, 1983;Swerdlow and Varshavsky, 1983), in part due to experimental discrepancies but also caused by an extrapolation of data obtained from welldefined components, like chicken erythrocyte mononucleosomes, to more complex systems. Nevertheless, studying nucleosomal organization within domains of transcribed chromatin requires understanding of these phenomena.…”

Section: Introductionmentioning

confidence: 99%

Chromatin from transcribed genes contains HMG17 only downstream from the starting point of transcription.

Dorbic

Wittig

1987

The EMBO Journal

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Monoclonal antibodies specific for the non‐histone chromosomal protein HMG17 were used to isolate oligonucleosomes from the transcriptionally active chromatin of chicken liver and oviduct. The distribution of HMG17 with respect to the coding region of three genes was analyzed in these oligonucleosomes by employing two independent experimental approaches. In the vitellogenin II gene (active in liver) and the lysozyme and ovalbumin genes (active in oviduct) HMG17 was found only downstream from the respective starting points of transcription. The transition from HMG17‐free to HMG17‐containing chromatin is located at the transcription start. This directly demonstrates that the distribution of an abundant nuclear protein correlates with the observation of moderate DNase I‐sensitivity in upstream regions and of high sensitivity in the coding regions of active genes.

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HMG 14/17 binding affinities and DNAase I sensitivities of nucleoprotein particles

Abstract: We show that ordinary (bulk) chicken erythrocyte nucleosomes are digested more rapidly by DNAase I when they are associated with high mobility group (HMG)

Cited by 30 publications

References 28 publications

Interaction between domains in chromosomal protein HMG-1.

Interaction between domains in chromosomal protein HMG-1.

Neither HMG-14a nor HMG-17 gene function is required for growth of chicken DT40 cells or maintenance of DNaseI-hypersensitive sites

Chromatin from transcribed genes contains HMG17 only downstream from the starting point of transcription.

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