High mobility group like chromosomal proteins from amebas of the acellular slime mold Physarum polycephalum

Biochemistry ◽  
1985 ◽  
Vol 24 (7) ◽  
pp. 1806-1812 ◽  
Author(s):  
Serge Cote ◽  
James M. Neelin ◽  
Dominick Pallotta
Keyword(s):  
Physarum Polycephalum ◽  
High Mobility ◽  
Slime Mold ◽  
High Mobility Group ◽  
Chromosomal Proteins

ADP-ribosylation of histones and acid-soluble, high mobility group like chromosomal proteins from Physarum polycephalum

1987 ◽  
Vol 65 (1) ◽  
pp. 81-85 ◽  
Author(s):  
G. G. Poirier ◽  
Serge Coté ◽  
Dominic Pallotta
Keyword(s):  
Gel Electrophoresis ◽  
Physarum Polycephalum ◽  
Polyacrylamide Gel Electrophoresis ◽  
Protein A ◽  
High Mobility ◽  
High Mobility Group ◽  
Chromosomal Proteins ◽  
Cellular Slime Mould ◽  
Adp Ribosylation ◽  
Cellular Slime

Nuclei from the cellular slime mould Physarum polycephalum were incubated with [32P]NAD. The chromosomal basic proteins were acid extracted and separated by two-dimensional polyacrylamide gel electrophoresis. After autoradiography the poly(ADP-ribosylated) proteins were identified. Histone H1 was the major acceptor. Histones H2B and H2A were significantly modified, although to a lesser extent than H1. In addition, the acid-soluble, high mobility group-like proteins AS-2 and AS-3 and the protein A-24 showed some modification. Histones H3 and H4 were not modified. The pattern of ADP-ribosylation did not change with NAD concentrations between 1 and 100 μM NAD.

High mobility group chromosomal proteins bind to AT-rich tracts flanking plant genes

1991 ◽  
Vol 16 (1) ◽  
pp. 95-104 ◽  
Author(s):  
Thomas J. Pedersen ◽  
Laura J. Arwood ◽  
Steven Spiker ◽  
Mark J. Guiltinan ◽  
William F. Thompson
Keyword(s):  
High Mobility ◽  
High Mobility Group ◽  
Chromosomal Proteins ◽  
Plant Genes

scholarly journals High mobility group (HMG) non-histone chromosomal proteins HMG1 and HMG2 are significant target antigens of perinuclear anti-neutrophil cytoplasmic antibodies in autoimmune hepatitis

Gut ◽  
1999 ◽  
Vol 44 (6) ◽  
pp. 867-873 ◽  
Author(s):  
J Sobajima ◽  
S Ozaki ◽  
H Uesugi ◽  
F Osakada ◽  
M Inoue ◽  
...  
Keyword(s):  
Chronic Hepatitis ◽  
Hepatitis C ◽  
Hepatitis B ◽  
Autoimmune Hepatitis ◽  
Chronic Hepatitis C ◽  
Chronic Hepatitis B ◽  
High Mobility ◽  
High Mobility Group ◽  
Enzyme Linked Immunosorbent Assay ◽  
Chromosomal Proteins

BACKGROUNDHigh mobility group (HMG) non-histone chromosomal proteins HMG1 and HMG2 have been identified as novel antigens of perinuclear anti-neutrophil cytoplasmic antibodies (p-ANCAs), and the existence of anti-HMG1 and anti-HMG2 antibodies in a population of patients with ulcerative colitis has been reported.AIMSTo investigate whether HMG1 and HMG2 are target antigens for p-ANCAs in autoimmune hepatitis (AIH).PATIENTSSerum samples from 28 patients with AIH, 44 patients with primary biliary cirrhosis (PBC), 27 patients with chronic hepatitis C, and 23 patients with chronic hepatitis B were tested.METHODSANCAs were detected by routine indirect immunofluorescence (IIF). Anti-HMG1 and anti-HMG2 antibodies were assayed by enzyme linked immunosorbent assay.RESULTSp-ANCAs were detected in 89% (25/28) of patients with AIH, 36% (16/44) of patients with PBC, 11% (3/27) of patients with chronic hepatitis C, and 13% (3/23) of patients with chronic hepatitis B. Anti-HMG1 and/or anti-HMG2 antibodies were detected in 89% (25/28) of patients with AIH, 70% (31/44) with PBC, 26% (7/27) with chronic hepatitis C, and 9% (2/23) with chronic hepatitis B. In AIH, anti-HMG1 and/or anti-HMG2 antibodies were detected in 96% (24/25) of p-ANCA positive patients. The p-ANCA staining pattern detected by IIF using sera from patients with AIH disappeared or decreased in titre after preincubation with a mixture of HMG1/HMG2. The presence and titres of those antibodies in AIH correlated significantly with those of p-ANCA, but not with those of anti-nuclear antibody or anti-smooth muscle antibody.CONCLUSIONSHMG1 and HMG2 are significant target antigens of p-ANCA in AIH.

scholarly journals Macronuclei and micronuclei in Tetrahymena thermophila contain high-mobility-group-like chromosomal proteins containing a highly conserved eleven-amino-acid putative DNA-binding sequence.

1991 ◽  
Vol 11 (1) ◽  
pp. 166-174 ◽  
Author(s):  
I G Schulman ◽  
T Wang ◽  
M Wu ◽  
J Bowen ◽  
R G Cook ◽  
...  
Keyword(s):  
Amino Acid ◽  
Dna Binding ◽  
Tetrahymena Thermophila ◽  
High Mobility ◽  
Amino Acid Sequences ◽  
High Mobility Group ◽  
Binding Motif ◽  
Hmg Proteins ◽  
Chromosomal Proteins ◽  
Conserved Sequence

HMG (high-mobility-group protein) B and HMG C are abundant nonhistone chromosomal proteins isolated from Tetrahymena thermophila macronuclei with solubilities, molecular weights, and amino acid compositions like those of vertebrate HMG proteins. Genomic clones encoding each of these proteins have been sequenced. Both are single-copy genes that encode single polyadenylated messages whose amounts are 10 to 15 times greater in growing cells than in starved, nongrowing cells. The derived amino acid sequences of HMG B and HMG C contain a highly conserved sequence, the HMG 1 box, found in vertebrate HMGs 1 and 2, and we speculate that this sequence may represent a novel, previously unrecognized DNA-binding motif in this class of chromosomal proteins. Like HMGs 1 and 2, HMGs B and C contain a high percentage of aromatic amino acids. However, the Tetrahymena HMGs are small, are associated with nucleosome core particles, and can be specifically extracted from macronuclei by elutive intercalation, properties associated with vertebrate HMGs 14 and 17, not HMGs 1 and 2. Thus, it appears that these Tetrahymena proteins have features in common with both of the major subgroups of higher eucaryotic HMG proteins. Surprisingly, a linker histone found exclusively in transcriptionally inactive micronuclei also has several HMG-like characteristics, including the ability to be specifically extracted from nuclei by elutive intercalation and the presence of the HMG 1 box. This finding suggests that at least in T. thermophila, proteins with HMG-like properties are not restricted to regions of transcriptionally active chromatin.

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