d-Cycloserine Inactivation ofd-Amino Acid Aminotransferase Leads to a Stable Noncovalent Protein Complex with an Aromatic Cycloserine-PLP Derivative

1998 ◽  
Vol 120 (10) ◽  
pp. 2268-2274 ◽  
Author(s):  
Daniel Peisach ◽  
David M. Chipman ◽  
Peter W. Van Ophem ◽  
James M. Manning ◽  
Dagmar Ringe
Keyword(s):  
Amino Acid ◽  
Protein Complex ◽  
Noncovalent Protein Complex ◽  
Noncovalent Protein

scholarly journals Humanizing the yeast origin recognition complex

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Clare S. K. Lee ◽  
Ming Fung Cheung ◽  
Jinsen Li ◽  
Yongqian Zhao ◽  
Wai Hei Lam ◽  
...  
Keyword(s):  
Amino Acid ◽  
Protein Complex ◽  
Origin Recognition Complex ◽  
Specific Binding ◽  
Life Cycles ◽  
Amino Acid Insertion ◽  
Evolutionarily Conserved ◽  
Transcriptional Start Sites ◽  
Eukaryote Genome ◽  
Origin Recognition

AbstractThe Origin Recognition Complex (ORC) is an evolutionarily conserved six-subunit protein complex that binds specific sites at many locations to coordinately replicate the entire eukaryote genome. Though highly conserved in structure, ORC’s selectivity for replication origins has diverged tremendously between yeasts and humans to adapt to vastly different life cycles. In this work, we demonstrate that the selectivity determinant of ORC for DNA binding lies in a 19-amino acid insertion helix in the Orc4 subunit, which is present in yeast but absent in human. Removal of this motif from Orc4 transforms the yeast ORC, which selects origins based on base-specific binding at defined locations, into one whose selectivity is dictated by chromatin landscape and afforded with plasticity, as reported for human. Notably, the altered yeast ORC has acquired an affinity for regions near transcriptional start sites (TSSs), which the human ORC also favors.

Detection of fos protein during osteogenesis by monoclonal antibodies

1988 ◽  
Vol 8 (5) ◽  
pp. 2251-2256
Author(s):  
P De Togni ◽  
H Niman ◽  
V Raymond ◽  
P Sawchenko ◽  
I M Verma
Keyword(s):  
Monoclonal Antibodies ◽  
Amino Acid ◽  
Indirect Immunofluorescence ◽  
Protein Complex ◽  
Synthetic Peptide ◽  
Immunohistochemical Staining ◽  
Nuclear Staining ◽  
Rat Embryos ◽  
Fos Protein ◽  
Modified Forms

We have generated monoclonal antibodies by using a synthetic peptide corresponding to amino acid positions 4 to 17 of the human fos protein. The antibodies detected both v- and c-fos proteins by immunoprecipitation, immunoblotting, and indirect immunofluorescence. The monoclonal antibodies not only identified the fos protein complex with the cellular 39-kilodalton protein, but also recognized the modified forms of the mouse, rat, and human fos proteins. In day-17 rat embryos, nuclear-staining fos protein could be identified in the cartilage by immunohistochemical staining.

scholarly journals Control of Amino Acid Homeostasis by a Ubiquitin Ligase-Coactivator Protein Complex

2017 ◽  
Vol 292 (9) ◽  
pp. 3827-3840 ◽  
Author(s):  
Damian Guerra ◽  
Sonia M. Chapiro ◽  
Réjane Pratelli ◽  
Shi Yu ◽  
Weitao Jia ◽  
...  
Keyword(s):  
Amino Acid ◽  
Ubiquitin Ligase ◽  
Protein Complex ◽  
Coactivator Protein ◽  
Amino Acid Homeostasis

scholarly journals A 36 kDa monomeric protein and its complex with a 10 kDa protein both isolated from bovine aorta are calpactin-like proteins that differ in their Ca2+-dependent calmodulin-binding and actin-severing properties

1988 ◽  
Vol 251 (3) ◽  
pp. 777-785 ◽  
Author(s):  
F Martin ◽  
J Derancourt ◽  
J P Capony ◽  
A Watrin ◽  
J C Cavadore
Keyword(s):  
Plasma Membrane ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Protein Complex ◽  
Actin Filaments ◽  
Thin Filament ◽  
Partial Amino Acid Sequence ◽  
Calmodulin Binding

Interaction of plasma membrane with the cytoskeleton involves a large number of proteins, among them a 36 kDa protein that was found to be involved in the interaction with actin filaments. We have isolated a 36 kDa protein from bovine aorta as a monomer and in a complex with a 10 kDa protein. Partial amino acid sequence determinations show that the 36 kDa and 10 kDa proteins isolated from bovine aorta are analogous to or identical with corresponding proteins purified from bovine intestine already described by Kristensen, Saris, Hunter, Hicks, Noonan, Glenney & Tack [(1986) Biochemistry 25, 4497-4503]. We report here that the association of the 10 kDa protein with the 36 kDa protein confers specific calmodulin-binding and actin-severing properties on the complex that are not possessed by the 36 kDa monomer alone. These findings suggest that the protein complex could be involved in thin-filament-related structures or could modulate some Ca2+-regulated events mediated by calmodulin.

scholarly journals The heparin–protein complex of ox liver capsule. Isolation and chemical characterization

1969 ◽  
Vol 112 (2) ◽  
pp. 167-172 ◽  
Author(s):  
A Serafini-Fracassini ◽  
J J Durward ◽  
L. Floreani
Keyword(s):  
Amino Acid ◽  
Column Chromatography ◽  
Catalytic Hydrogenation ◽  
Protein Complex ◽  
Amino Acid Analysis ◽  
Chemical Characterization ◽  
Isolation And Purification ◽  
Liver Capsule ◽  
Heparin Fractions ◽  
Good Agreement

1. A procedure for the isolation and purification of the heparin–protein complex from ox liver capsule, based on the solubility properties of mucopolysaccharide–cetylpyridinium complexes, is described. 2. The yield of the heparin–protein complex with this method averages 35mg./100g. of dry ox liver capsule. 3. The results of analyses on the polysaccharide show good agreement with values previously published for purified heparin fractions. 4. The amino acid analysis of the protein component shows several similarities to that of chondromucoprotein. 5. The results of β-carbonyl elimination, either with or without catalytic hydrogenation, and column chromatography after β-elimination, show that the polysaccharide is covalently bound to the protein.

scholarly journals The composition of peptidochitodextrins from sarcophagid puparial cases

1971 ◽  
Vol 125 (3) ◽  
pp. 703-716 ◽  
Author(s):  
H. Lipke ◽  
T. Geoghegan
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Protein Complex ◽  
Covalent Bonds ◽  
Aromatic Residues ◽  
Similar Molecular Weight ◽  
X Ray ◽  
Molecular Weights ◽  
Physical Interactions ◽  
The Stability

1. N-Bromosuccinimide cleaved proteins and pigments from fly puparia, increasing the chitin:protein ratio from 0.5 to 1.5. The product afforded subfractions (ratio 5:1) of molecular weights of 1200 and 1600 devoid of aromatic residues and N-terminal β-alanine, direct aryl links between polysaccharide chains being discounted. 2. The chitin–protein complex decreased in molecular weight when treated with Pronase, which suggested polypeptide bridges within the native chitin micelle. The limit dextrins generated by chitinase were mixtures of unsubstituted dextrins and peptidylated oligosaccharides, with the former predominating. 3. Peptidochitodextrins of similar molecular weight but markedly different solubility were prepared, which were indistinguishable with respect to amino acid, glucosamine, acetyl, X-ray or infrared characteristics. It is suggested that physical interactions contribute to the stability of the integument in addition to the covalent bonds that form during sclerotization.

scholarly journals The mutation Arg (53)----Trp causes von Willebrand disease Normandy by abolishing binding to factor VIII. Studies with recombinant von Willebrand factor

Blood ◽  
1992 ◽  
Vol 79 (3) ◽  
pp. 563-567 ◽  
Author(s):  
S Jorieux ◽  
EA Tuley ◽  
C Gaucher ◽  
C Mazurier ◽  
JE Sadler
Keyword(s):  
Amino Acid ◽  
Factor Viii ◽  
Von Willebrand Factor ◽  
Protein Complex ◽  
Von Willebrand Disease ◽  
Cho Cell ◽  
Fviii Activity ◽  
New Variant ◽  
Von Willebrand ◽  
Willebrand Factor

Abstract von Willebrand factor (vWF) and factor VIII (FVIII) circulate in plasma as a noncovalently linked protein complex. The FVIII/vWF interaction is required for the stabilization of procoagulant FVIII activity. Recently, we reported a new variant of von Willebrand disease (vWD) tentatively named “Normandy,” characterized by plasma vWF that appears to be structurally and functionally normal except that it does not bind FVIII. Three patients from one family were found to be homozygous for a C----T transition at codon 816 converting Arg 53 to Trp in the mature vWF subunit. To firmly establish a causal relationship between this missense mutation and vWD Normandy phenotype, we have characterized the corresponding recombinant mutant vWF(R53W). Expressed in COS-7 cells or CHO cell lines, normal vWF and vWF(R53W) were processed and formed multimers with equal efficiency. However, vWF(R53W) exhibited the same defect in FVIII binding as did plasma vWF from patients with vWD Normandy, confirming that this mutation is responsible for the vWD Normandy phenotype. These results illustrate the importance of Arg 53 of the mature vWF subunit for the binding of FVIII to vWF, and identify an amino acid residue within a disulfide loop not previously known to be involved in this interaction.

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