scholarly journals The tubulin-binding sequence of brain microtubule-associated proteins, tau and MAP-2, is also involved in actin binding

1990 ◽  
Vol 269 (1) ◽  
pp. 61-64 ◽  
Author(s):  
I Correas ◽  
R Padilla ◽  
J Avila
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Affinity Chromatography ◽  
Binding Sites ◽  
Synthetic Peptide ◽  
Actin Binding ◽  
Microtubule Associated Proteins ◽  
Tubulin Binding ◽  
Associated Proteins ◽  
Binding Sequence

The interaction of actin with a synthetic peptide which corresponds to one of the repeated tubulin-binding sites present in tau and MAP-2 (microtubule-associated protein 2) proteins has been analysed. The analysis, which uses affinity chromatography of G-actin on a column containing the synthetic peptide, and the co-sedimentation and co-localization of F-actin and the peptide (as determined by immunoelectron microscopy), indicates that the part of the amino acid sequence of tau involved in the binding of tubulin is also involved in actin binding.

Blackjack, a novel protein associated with microtubules in embryonic neurons

1996 ◽  
Vol 109 (6) ◽  
pp. 1497-1507
Author(s):  
K.R. Zachow ◽  
D. Bentley
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Predicted Amino Acid Sequence ◽  
Microtubule Associated Proteins ◽  
Amino Terminal ◽  
Molecular Features ◽  
Associated Proteins ◽  
Carboxy Terminal ◽  
Novel Protein ◽  
Embryonic Neurons

Microtubule-associated proteins can influence the organization, stability and dynamics of microtubules. We characterize a novel protein that associates with microtubules as assessed by immunofluorescence, immunoelectron microscopy, and co-sedimentation. The protein is expressed heavily in embryonic neurons and, to a lesser extent, in epithelial and mesodermal cells. The cDNA sequence predicts a protein of 1,547 amino acids and approximately 170 kDa. Immunoblot of embryo lysate demonstrates bands of approximately 240 and 260 kDa. The predicted amino acid sequence contains 77 potential serine/threonine phosphorylation sites. A distinctive feature is a predicted alpha-helical central domain comprising 21 identical repeats of an 11 amino acid sequence (PLEELRKDAAE). The protein is thermostable and has two major charge-domains: the amino-terminal 80% has an estimated pI of 4.0 and the carboxy-terminal 20%, a pI of 12.2. The protein shares several general biochemical and molecular features of MAPs, but its sequence is not similar to that of any described MAP.

scholarly journals Common and distinct tubulin binding sites for microtubule-associated proteins.

1986 ◽  
Vol 83 (19) ◽  
pp. 7162-7166 ◽  
Author(s):  
U. Z. Littauer ◽  
D. Giveon ◽  
M. Thierauf ◽  
I. Ginzburg ◽  
H. Ponstingl
Keyword(s):  
Binding Sites ◽  
Microtubule Associated Proteins ◽  
Tubulin Binding ◽  
Associated Proteins

Nucleoid-associated proteins in Crenarchaea

2011 ◽  
Vol 39 (1) ◽  
pp. 116-121 ◽  
Author(s):  
Rosalie P.C. Driessen ◽  
Remus Th. Dame
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Structural Effect ◽  
Chromatin Organization ◽  
Large Set ◽  
Chromosomal Dna ◽  
Amino Acid Sequence Level ◽  
Generic Level ◽  
Architectural Proteins ◽  
Associated Proteins

Architectural proteins play an important role in compacting and organizing the chromosomal DNA in all three kingdoms of life (Eukarya, Bacteria and Archaea). These proteins are generally not conserved at the amino acid sequence level, but the mechanisms by which they modulate the genome do seem to be functionally conserved across kingdoms. On a generic level, architectural proteins can be classified based on their structural effect as DNA benders, DNA bridgers or DNA wrappers. Although chromatin organization in archaea has not been studied extensively, quite a number of architectural proteins have been identified. In the present paper, we summarize the knowledge currently available on these proteins in Crenarchaea. By the type of architectural proteins available, the crenarchaeal nucleoid shows similarities with that of Bacteria. It relies on the action of a large set of small, abundant and generally basic proteins to compact and organize their genome and to modulate its activity.

Plasmin-platelet interaction involves cleavage of functional thrombin receptor

1996 ◽  
Vol 271 (1) ◽  
pp. C54-C60 ◽  
Author(s):  
M. Kimura ◽  
T. T. Andersen ◽  
J. W. Fenton ◽  
W. F. Bahou ◽  
A. Aviv
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Platelet Activation ◽  
Synthetic Peptide ◽  
Time Dependent ◽  
Thrombin Receptor ◽  
Amino Acid Residues ◽  
Enzymatic Action ◽  
High Concentrations ◽  
Inhibition Of Thrombin

We tested the hypothesis that the inhibition of thrombin-induced platelet activation by plasmin is mediated via the enzymatic action of plasmin on the functional thrombin receptor. We monitored the binding of the anti-thrombin receptor antibody [anti-TR-(34-46)] to platelets; this binding is sensitive to the cleavage of the thrombin receptor at amino acid residues Arg-41 to Ser-42. Plasmin inhibited anti-TR-(34-46) binding in dose- and time-dependent manners. The inactive synthetic peptide with the amino acid sequence 40-55 of the thrombin receptor (D-FPRSFLLRNPNDKYEPF) was similarly cleaved by thrombin and plasmin to an active peptide (SFLLRNPNDKYEPF) that produced robust cytosolic Ca2+ responses. At high concentrations, plasmin itself can activate platelets. We explored this effect with the use of anti-TR-(1-160). This antibody abolished the cytosolic Ca2+ responses to thrombin and to the thrombin receptor-activating peptide SFLLRN but did not attenuate the plasmin-induced cytosolic Ca2+ response. Thus plasmin inhibits thrombin-evoked platelet activation by cleaving the thrombin receptor, but the plasmin-induced cytosolic Ca2+ response is not due to the generation of the tethered peptide of the thrombin receptor.

Abstract 4535: The mTOR complex 2 promotes glioblastoma migration via the interactions with multiple actin-binding and microtubule-associated proteins

2019 ◽  
Author(s):  
Naphat Chantaravisoot ◽  
Piriya Wongkongkathep ◽  
Narawit Pacharakullanon ◽  
Fuyuhiko Tamanoi ◽  
Joseph A. Loo ◽  
...  
Keyword(s):  
Actin Binding ◽  
Microtubule Associated Proteins ◽  
Associated Proteins

Expression of Na+-d-glucose cotransporter in brush-border membrane of the chicken intestine

1999 ◽  
Vol 276 (2) ◽  
pp. R627-R631 ◽  
Author(s):  
Carles Garriga ◽  
Nativitat Rovira ◽  
Miquel Moretó ◽  
Joana M. Planas
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Western Blot ◽  
Brush Border ◽  
Synthetic Peptide ◽  
Brush Border Membrane ◽  
Polyclonal Antibodies ◽  
Membrane Vesicles ◽  
Dependent Transport

We have studied the expression of Na+-d-glucose cotransporter in brush-border membrane vesicles (BBMVs) of chicken enterocytes to correlate the changes in the apical Na+-dependent transport with the changes in the amounts of transporter determined by Western blot analysis. Two different rabbit polyclonal antibodies were used simultaneously. The antibody raised against amino acids 564–575 of the deduced amino acid sequence of rabbit intestinal SGLT-1 ( antibody 1) specifically detects a single 75-kDa band in the three segments, and this band disappeared when the antibody was preabsorbed with the antigenic peptide. The antibody raised against the synthetic peptide corresponding to amino acids 402–420 of the same protein ( antibody 2) only reacts with jejunal and ileal samples, but no signal is found in BBMVs of rectum. Only when antibody 1 was used was there a linear correlation between the maximal transport rates of hexoses in BBMVs and the relative protein amounts determined by Western blot. These results indicate that the Na+-d-glucose cotransport in the jejunum, the ileum, and the rectum of chickens is due to an SGLT-1 type protein.

Purification and structural characterization of ovine placental lactogen

1990 ◽  
Vol 126 (1) ◽  
pp. 141-149 ◽  
Author(s):  
W. C. Warren ◽  
R. Liang ◽  
G. G. Krivi ◽  
N. R. Siegel ◽  
R. V. Anthony
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Structural Characterization ◽  
Binding Sites ◽  
Untranslated Region ◽  
Fetal Liver ◽  
Radioreceptor Assay ◽  
Placental Lactogen ◽  
Predicted Amino Acid Sequence ◽  
Cdna Clones

ABSTRACT Discrepancies exist in the reported purity and biological activity of ovine placental lactogen (oPL), and little structural characterization has been reported. Ovine PL was purified from fetal cotyledonary tissue (day 100 of gestation) by monitoring activity with a recombinant bovine GH (bGH) liver radioreceptor assay. Two hundred grams of tissue yielded 4·2 mg of oPL, with an ∼ 1000-fold purification of oPL specific activity following initial tissue extraction. The oPL was radioiodinated and used in an ovine fetal liver (day 100 of gestation) radioreceptor assay to examine competitive displacement of oPL, ovine GH (oGH) and ovine prolactin (oPRL). The potency of oPL (ED50 = 0·18 nmol/l; ED50 is the quantity of ligand necessary to displace 50% of specifically bound 125I-labelled oPL) was greater than that of oGH (ED50 = 4·1 nmol/l) and oPRL (ED50 = 1·1 μmol/l) in competing for 125I-labelled oPL-binding sites. Attempts to sequence the NH2 terminus of oPL by vapour-phase sequencing indicated that the NH2 terminus was blocked. Purified oPL was subjected to trypsin and CnBr digestion, and two CnBr and six tryptic peptides were sequenced. The peptide sequences were compared with other PLs, oPRL and bGH for sequence similarity, and found to be most similar to bovine PL (bPL; 68% overall identity) and oPRL (47% overall identity). Complementary DNA (cDNA) clones were isolated for oPL by screening a λZAP cDNA library with a cDNA coding for bPL. Three cDNAs were nucleotide sequenced, and their combined sequence included 41 nucleotides of 5'-untranslated region, the complete coding region of pre-oPL (708 nucleotides) and a portion of the 3' untranslated region (158 nucleotides). The predicted amino acid sequence derived from the nucleotide sequence confirmed homology to bPL (67%) and oPRL (48%). Little amino acid sequence existed with other PLs (≤29%) or GH proteins (≤27%). These results suggest that oPL and oGH are more biologically similar in their ability to compete for fetal liver binding sites, but that oPL is structurally more similar to oPRL. Elucidation of exact structure–function relationships for oPL will, however, require further investigation. Journal of Endocrinology (1990) 126, 141–149

scholarly journals Identification of microtubule-associated proteins in the centrosome, spindle, and kinetochore of the early Drosophila embryo.

1989 ◽  
Vol 109 (6) ◽  
pp. 2977-2991 ◽  
Author(s):  
D R Kellogg ◽  
C M Field ◽  
B M Alberts
Keyword(s):  
Affinity Chromatography ◽  
Mitotic Spindle ◽  
Polyclonal Antibodies ◽  
Drosophila Embryo ◽  
Microtubule Cytoskeleton ◽  
Microtubule Associated Proteins ◽  
Early Drosophila Embryo ◽  
Individual Mouse ◽  
Associated Proteins

We have developed affinity chromatography methods for the isolation of microtubule-associated proteins (MAPs) from soluble cytoplasmic extracts and have used them to analyze the cytoskeleton of the early Drosophila embryo. More than 50 Drosophila embryo proteins bind to microtubule affinity columns. To begin to characterize these proteins, we have generated individual mouse polyclonal antibodies that specifically recognize 24 of them. As judged by immunofluorescence, some of the antigens localize to the mitotic spindle in the early Drosophila embryo, while others are present in centrosomes, kinetochores, subsets of microtubules, or a combination of these structures. Since 20 of the 24 antibodies stain microtubule structures, it is likely that most of the proteins that bind to our columns are associated with microtubules in vivo. Very few MAPS seem to be identically localized in the cell, indicating that the microtubule cytoskeleton is remarkably complex.

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