scholarly journals Calcium-dependent ADP-ribosylation of high-mobility-group I (HMGI) proteins

1996 ◽  
Vol 317 (3) ◽  
pp. 865-870 ◽  
Author(s):  
Vincenzo GIANCOTTI ◽  
Antonella BANDIERA ◽  
Chiara SINDICI ◽  
Laura PERISSIN ◽  
Colyn CRANE-ROBINSON
Keyword(s):  
High Mobility ◽  
High Mobility Group ◽  
Micrococcal Nuclease ◽  
Calcium Dependent ◽  
Lung Carcinoma Cells ◽  
Group I ◽  
Micrococcal Nuclease Digestion ◽  
Nuclease Digestion ◽  
Full Complement ◽  
Lewis Lung Carcinoma Cells

Micrococcal nuclease digestion of nuclei from mouse Lewis lung carcinoma cells releases a protein mixture into the supernatant that lacks histone H1 and contains a full complement of high-mobility-group I (HMGI) proteins (i.e. I, Y and I-C). This implies that all three HMGI proteins are localized at the nuclease-sensitive regions of active chromatin. It is also shown that if Ca2+ ions are present in the nuclear incubation buffer (with or without exogenous nuclease), all three HMGI proteins become ADP-ribosylated. We propose that this modification of HMGI family proteins is part of the general poly(ADP-ribosyl)ation that accompanies DNA damage in apoptosis and other processes.

scholarly journals Studies on the high-mobility-group non-histone proteins from hen oviduct

1979 ◽  
Vol 181 (3) ◽  
pp. 585-591 ◽  
Author(s):  
C S Teng ◽  
G K Andrews ◽  
C T Teng
Keyword(s):  
Polyacrylamide Gel Electrophoresis ◽  
High Mobility ◽  
High Mobility Group ◽  
Micrococcal Nuclease ◽  
Hmg Proteins ◽  
Deoxyribonuclease I ◽  
Micrococcal Nuclease Digestion ◽  
Calf Thymus ◽  
Nuclease Digestion ◽  
Limited Digestion

Nuclear high-mobility-group (HMG) proteins were isolated from hen oviduct. These were proteins HMG-1, −2, −3, −14 and −17, which are equivalent to the classification of calf thymus HMG proteins. Hen oviduct proteins HMG-1 and −2 were individually isolated by HCIO4.extraction and CM-Sephadex chromatographic separation. Their mol.wts. were determined as 28 000 and 27 000, respectively. The proteins have a high content of acidic and basic amino acids. The association of proteins HMG-1 and −2 with the genome of hen oviduct nuclei was probed by a limited digestion with nucleases. Hen oviduct nuclei were incubated with deoxyribonuclease I or micrococcal nuclease until 10% of the DNA was digested. The nuclear suspension was centrifuged and the contents of proteins HMG-1 and −2 in the supernatant and sediment fractions were analysed by polyacrylamide-gel electrophoresis. HMG proteins were found to be preferentially released by micrococcal-nuclease digestion rather than by deoxyribonuclease I.

Analysis of high mobility group I(Y) [HMGI(Y)] proteins expression in pancreatic neoplasms

2000 ◽  
Vol 118 (4) ◽  
pp. A271
Author(s):  
Nobutsugu Abe ◽  
Takashi Watanabe ◽  
Masanori Sugiyama ◽  
Yutaka Atomi
Keyword(s):  
Pancreatic Neoplasms ◽  
High Mobility ◽  
High Mobility Group ◽  
Group I

scholarly journals Human SWI/SNF Generates Abundant, Structurally Altered Dinucleosomes on Polynucleosomal Templates

2005 ◽  
Vol 25 (24) ◽  
pp. 11156-11170 ◽  
Author(s):  
Natalia P. Ulyanova ◽  
Gavin R. Schnitzler
Keyword(s):  
Cell Cycle Control ◽  
Micrococcal Nuclease ◽  
Asymmetric Structures ◽  
Micrococcal Nuclease Digestion ◽  
Evolutionarily Conserved ◽  
Nuclease Digestion ◽  
Transcriptional Memory ◽  
Altered Form ◽  
Regulatory Functions ◽  
Negative Supercoils

ABSTRACT Human SWI/SNF (hSWI/SNF) is an evolutionarily conserved ATP-dependent chromatin remodeling complex required for transcriptional regulation and cell cycle control. The regulatory functions of hSWI/SNF are correlated with its ability to create a stable, altered form of chromatin that constrains fewer negative supercoils than normal. Our current studies indicate that this change in supercoiling is due to the conversion of up to one-half of the nucleosomes on polynucleosomal arrays into asymmetric structures, termed “altosomes,” each composed of two histone octamers and bearing an asymmetrically located region of nuclease-accessible DNA. Altosomes can be formed on chromatin containing the abundant mammalian linker histone H1 and have a unique micrococcal nuclease digestion footprint that allows their position and abundance on any DNA sequence to be measured. Over time, altosomes spontaneously revert to structurally normal but improperly positioned nucleosomes, suggesting a novel mechanism for transcriptional attenuation as well as transcriptional memory following hSWI/SNF action.

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