Non-random reconstitution of HMG1 and HMG2 in chromatin. Determination of the histone contacts

Jordi Bernués; Enrique Querol

doi:10.1016/0167-4781(89)90169-3

Non-random reconstitution of HMG1 and HMG2 in chromatin. Determination of the histone contacts

Jordi Bernués, Enrique Querol

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Abstract

We have studied how non-histone proteins HMG1 and HMG2 interact with rat liver chromatin using reconstitution and chemical cross-linking procedures. Both proteins were found to associate to chromatin only to some extent and always with a marked preference for short oligonucleosomes, mainly mono- and dinucleosomes. However, a slight reconstitution with the long polynucleosomal fraction can be observed in H1-depleted chromatin. Reconstitution is non-random and a clear preference for regions highly sensitive to staphylococcal nuclease (EC 3.1.31.1) is observed. Chemical cross-linking has allowed us to identify H1, H2A and H2B as the histones contacted by HMG1 and HMG2 upon reconstitution. Also, we present evidence that HMG2 and HMG2 interact with the nucleosomal particle without replacing H1 or any other histone. © 1989.

Original language	English
Pages (from-to)	52-61
Journal	Biochimica et biophysica acta. General subjects
Volume	0
Issue number	1008
DOIs	https://doi.org/10.1016/0167-4781(89)90169-3
Publication status	Published - 1 Jun 1989

Keywords

(Calf thymus)
Chromatin-protein interaction
High mobility group protein
Nonhistone protein

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10.1016/0167-4781(89)90169-3

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title = "Non-random reconstitution of HMG1 and HMG2 in chromatin. Determination of the histone contacts",

abstract = "We have studied how non-histone proteins HMG1 and HMG2 interact with rat liver chromatin using reconstitution and chemical cross-linking procedures. Both proteins were found to associate to chromatin only to some extent and always with a marked preference for short oligonucleosomes, mainly mono- and dinucleosomes. However, a slight reconstitution with the long polynucleosomal fraction can be observed in H1-depleted chromatin. Reconstitution is non-random and a clear preference for regions highly sensitive to staphylococcal nuclease (EC 3.1.31.1) is observed. Chemical cross-linking has allowed us to identify H1, H2A and H2B as the histones contacted by HMG1 and HMG2 upon reconstitution. Also, we present evidence that HMG2 and HMG2 interact with the nucleosomal particle without replacing H1 or any other histone. {\textcopyright} 1989.",

keywords = "(Calf thymus), Chromatin-protein interaction, High mobility group protein, Nonhistone protein",

author = "Jordi Bernu{\'e}s and Enrique Querol",

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doi = "10.1016/0167-4781(89)90169-3",

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TY - JOUR

T1 - Non-random reconstitution of HMG1 and HMG2 in chromatin. Determination of the histone contacts

AU - Bernués, Jordi

AU - Querol, Enrique

PY - 1989/6/1

Y1 - 1989/6/1

N2 - We have studied how non-histone proteins HMG1 and HMG2 interact with rat liver chromatin using reconstitution and chemical cross-linking procedures. Both proteins were found to associate to chromatin only to some extent and always with a marked preference for short oligonucleosomes, mainly mono- and dinucleosomes. However, a slight reconstitution with the long polynucleosomal fraction can be observed in H1-depleted chromatin. Reconstitution is non-random and a clear preference for regions highly sensitive to staphylococcal nuclease (EC 3.1.31.1) is observed. Chemical cross-linking has allowed us to identify H1, H2A and H2B as the histones contacted by HMG1 and HMG2 upon reconstitution. Also, we present evidence that HMG2 and HMG2 interact with the nucleosomal particle without replacing H1 or any other histone. © 1989.

AB - We have studied how non-histone proteins HMG1 and HMG2 interact with rat liver chromatin using reconstitution and chemical cross-linking procedures. Both proteins were found to associate to chromatin only to some extent and always with a marked preference for short oligonucleosomes, mainly mono- and dinucleosomes. However, a slight reconstitution with the long polynucleosomal fraction can be observed in H1-depleted chromatin. Reconstitution is non-random and a clear preference for regions highly sensitive to staphylococcal nuclease (EC 3.1.31.1) is observed. Chemical cross-linking has allowed us to identify H1, H2A and H2B as the histones contacted by HMG1 and HMG2 upon reconstitution. Also, we present evidence that HMG2 and HMG2 interact with the nucleosomal particle without replacing H1 or any other histone. © 1989.

KW - (Calf thymus)

KW - Chromatin-protein interaction

KW - High mobility group protein

KW - Nonhistone protein

U2 - 10.1016/0167-4781(89)90169-3

DO - 10.1016/0167-4781(89)90169-3

M3 - Article

SN - 0304-4165

VL - 0

SP - 52

EP - 61

JO - Biochimica et biophysica acta. General subjects

JF - Biochimica et biophysica acta. General subjects

IS - 1008

ER -

Non-random reconstitution of HMG1 and HMG2 in chromatin. Determination of the histone contacts

Abstract

Keywords

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