Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Two new low-molecular-weight acidic proteins from calf thymus nuclei that resemble HMG (high-mobility-group) proteins 14 and 17.

ABSTRACT: Two new, closely similar, acidic proteins were extracted and purified from calf thymus and designated AP-X and AP-Y (acidic proteins X and Y). They contain about 33% acidic residues, mostly non-amidated, and 20% lysine, but no arginine, tyrosine, histidine or tryptophan. There is a single phenylalanine residue in a molecular weight of approx. 5000. Circular dichroism and proton nuclear magnetic resonance show that they do not take up secondary or tertiary structure in free solution, as expected from the low content of hydrophobic amino acids. They appear structurally related to the high-mobility-group proteins HMG 14 and 17. Controlled extraction experiments indicate that proteins AP-X and AP-Y are at least partially located in the calf thymus nucleus.

SUBMITTER: Cary PD

PROVIDER: S-EPMC1153892 | biostudies-other | 1982 Dec

REPOSITORIES: biostudies-other

ACCESS DATA

Json Xml

Similar Datasets

HMG (high-mobility-group)-14/17-like proteins in calf thyroid. Thyrotropin-dependent phosphorylation and comparison with calf thymus proteins.

Project description:Two-dimensional polyacrylamide-gel electrophoresis of acid extracts of thyroid and thymus tissue, and of thyroid nuclei, revealed the presence of three HClO4-soluble nuclear proteins, PS.1, PS.2 and PS.3, whose electrophoretic mobilities closely resembled those of HMG (high-mobility-group) proteins 14 and 17. PS.1 co-migrated with HMG 14 on CM-Sephadex column chromatography. Like HMG 14, PS.2 and PS.3 were phosphorylated in calf thyroid slices; 32P-labelling of PS.3 was stimulated by thyrotropin. Thyrotropin also induced a rapid increase in the labelling of A5, an HMG-14/17-like protein found in whole calf thyroid and thymus tissue, but not in thyroid nuclei.

| S-EPMC1152447 | biostudies-other

Heterogeneity of proteins resembling high-mobility-group protein HMG-T in trout testes nuclei.

Project description:Two proteins, HMG-T1 and HMG-T2, with electrophoretic mobilities and compositions similar to those of protein HMG-T, were isolated from trout testes nuclei. The isoelectric points of proteins HMG-T1, HMG-T2 and HMG-T differ. The first 20 residues of protein HMG-T2 have been sequenced and differ from protein HMG-T by only one residue.

| S-EPMC1162261 | biostudies-other

Cysteine in calf-thymus histones.

Project description:1. Calf-thymus histones contain cysteine, which is present almost entirely in the arginine-rich fraction F3 to the extent of about 1mole in 15000g. weight of the histone. 2. The cysteine in fraction F3 is readily available to thiol reagents and the protein yields an approximately equivalent amount of cysteic acid on oxidation with performic acid.

| S-EPMC1264744 | biostudies-other

The isolation, characterization and partial sequence of a peptide rich in glutamic acid and aspartic acid (HGA-2 peptide) from calf thymus non-histone chromosomal protein HMG 2. Comparison with a similar peptide (HGA-1 peptide) from calf thymus non-histone chromosomal protein HMG 1.

Project description:A 41-residue peptide (HGA-2) containing a continuous sequence of 35 glutamic and aspartic residues was isolated from non-histone chromosomal protein HMG 2. This highly acidic peptide is compared with a similar peptide (HGA-1) isolated from non-histone chromosomal protein HMG 1.

| S-EPMC1186617 | biostudies-other

Conformation and Rheological Properties of Calf-Thymus DNA in Solution.

Project description:Studies of DNA molecule behavior in aqueous solutions performed through different approaches allow assessment of the solute-solvent interactions and examination of the strong influence of conformation on its physicochemical properties, in the presence of different ionic species and ionic concentrations. Firstly, the conformational behavior of calf-thymus DNA molecules in TE buffer solution is presented as a function of temperature. Secondly, their rheological behavior is discussed, as well as the evidence of the critical concentrations, i.e., the overlap and the entanglement concentrations (C* and Ce, respectively) from steady state flow and oscillatory dynamic shear experiments. The determination of the viscosity in the Newtonian plateau obtained from flow curves η ( ) allows estimation of the intrinsic viscosity and the specific viscosities at zero shear when C[η] < 40. At end, a generalized master curve is obtained from the variation of the specific viscosity as a function of the overlap parameter C[η]. The variation of the exponent s obtained from the power law η~ -s for both flow and dynamic results is discussed in terms of Graessley's analysis. In the semi-dilute regime with entanglements, a dynamic master curve is obtained as a function of DNA concentration (CDNA > 2.0 mg/mL) and temperature (10 °C < T < 40 °C).

| S-EPMC6432584 | biostudies-literature

Both high mobility group (HMG)-boxes and the acidic tail of HMGB1 regulate recombination-activating gene (RAG)-mediated recombination signal synapsis and cleavage in vitro.

Project description:RAG-1 and RAG-2 initiate V(D)J recombination through synapsis and cleavage of a 12/23 pair of V(D)J recombination signal sequences (RSS). RAG-RSS complex assembly and activity in vitro is promoted by high mobility group proteins of the "HMG-box" family, exemplified by HMGB1. How HMGB1 stimulates the DNA binding and cleavage activity of the RAG complex remains unclear. HMGB1 contains two homologous HMG-box DNA binding domains, termed A and B, linked by a stretch of basic residues to a highly acidic C-terminal tail. To identify determinants of HMGB1 required for stimulation of RAG-mediated RSS binding and cleavage, we prepared an extensive panel of mutant HMGB1 proteins and tested their ability to augment RAG-mediated RSS binding and cleavage activity. Using a combination of mobility shift and in-gel cleavage assays, we find that HMGB1 promotes RAG-mediated cleavage largely through the activity of box B, but optimal stimulation requires a functional A box tethered in the correct orientation. Box A or B mutants fail to promote RAG synaptic complex formation, but this defect is alleviated when the acidic tail is removed from these mutants.

| S-EPMC5992625 | biostudies-literature

Protein kinase C activation by acidic proteins including 14-3-3.

Project description:14-3-3 proteins may function as adapter or scaffold proteins in signal transduction pathways. We reported previously that several 14-3-3 isotypes bind to protein kinase C (PKC)-zeta and facilitate coupling of PKC-zeta to Raf-1 [van der Hoeven, van der Wal, Ruurs, van Dijk and van Blitterswijk (2000) Biochem. J. 345, 297-306], an event that boosts the mitogen-activated protein kinase (ERK) pathway in Rat-1 fibroblasts. The present work investigated whether bound 14-3-3 would affect PKC-zeta activity. Using recombinant 14-3-3 proteins and purified PKC-zeta in a convenient, newly developed in vitro kinase assay, we found that 14-3-3 proteins stimulated PKC-zeta activity in a dose-dependent fashion up to approx. 2.5-fold. Activation of PKC-zeta by 14-3-3 isotypes was unrelated to their mutual affinity, estimated by co-immunoprecipitation from COS cell lysates. Accordingly, PKC-zeta with a defective (point-mutated) 14-3-3-binding site, showed the same 14-3-3-stimulated activity as wild-type PKC-zeta. As 14-13-3 proteins are acidic, we tested several other acidic proteins, which turned out to stimulate PKC-zeta activity in a similar fashion, whereas neutral or basic proteins did not. These effects were not restricted to the atypical PKC-zeta, but were also found for classical PKC. Together, the results suggest that the stimulation of PKC activity by 14-3-3 proteins is non-specific and solely due to the acidic nature of these proteins, quite similar to that known for acidic lipids.

| S-EPMC1221016 | biostudies-other

Non-interacting proteins may resemble interacting proteins: prevalence and implications.

Project description:The vast majority of proteins do not form functional interactions in physiological conditions. We have considered several sets of protein pairs from S. cerevisiae with no functional interaction reported, denoted as non-interacting pairs, and compared their 3D structures to available experimental complexes. We identified some non-interacting pairs with significant structural similarity with experimental complexes, indicating that, even though they do not form functional interactions, they have compatible structures. We estimate that up to 8.7% of non-interacting protein pairs could have compatible structures. This number of interactions exceeds the number of functional interactions (around 0.2% of the total interactions) by a factor 40. Network analysis suggests that the interactions formed by non-interacting pairs with compatible structures could be particularly hazardous to the protein-protein interaction network. From a structural point of view, these interactions display no aberrant structural characteristics, and are even predicted as relatively stable and enriched in potential physical interactors, suggesting a major role of regulation to prevent them.

| S-EPMC5289270 | biostudies-literature

N-Terminal acetyl-peptides from two calf thymus histones.

Project description:1. The same N-terminal peptide was isolated from two major calf thymus histone fractions, F2al and F2a2. 2. The structure of the peptides is N-acetylseryl-glycyl-arginine, and the yields account for most of the N-acetyl groups previously found in these histones. 3. Some other peptides not giving a ninhydrin reaction were also investigated.

| S-EPMC1198638 | biostudies-other

Interaction of quinacrine mustard with calf thymus histone fractions.

Project description:1. Interactions of histone fractions with quinacrine mustard were investigated by fluorimetry and spectrophotometry and the results were interpreted with the aid of thinlayer chromatography. 2. Characteristic differences were found between the various histone fractions of calf thymus. The conditions that favoured histone conformational changes and aggregation, also favoured interaction between histones and the dye; low concentrations of SO(4) (2-) brought about more interaction than did Cl(-); urea, guanidinium and iodide ions were inhibitory to binding. 3. Changes in the physical state of all the quinacrine mustard-protein complexes occurred as a function of ionic strength and pH. The most salt-dependent interaction was found in the arginine-rich histone fraction. 4. The interaction of the calf thymus histone fractions with quinacrine mustard was compared with the interaction of bovine plasma albumin and protamine with quinacrine mustard. 5. The relationship between dye-binding and the aggregation of histone fractions was discussed.

| S-EPMC1177535 | biostudies-other

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data