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  • Charge-based interaction conserved within histone H3 lysine 4 (H3K4) methyltransferase complexes is needed for protein stability, histone methylation, and gene expression ... 22147691

    Histone H3 lysine 4 (H3K4) methyltransferases are conserved from yeast to humans, assemble in multisubunit complexes, and are needed to regulate gene expression. The yeast H3K4 methyltransferase complex, Set1 complex or complex of proteins associated with Set1 (COMPASS), consists of Set1 and conserved Set1-associated proteins: Swd1, Swd2, Swd3, Spp1, Bre2, Sdc1, and Shg1. The removal of the WD40 domain-containing subunits Swd1 and Swd3 leads to a loss of Set1 protein and consequently a complete loss of H3K4 methylation. However, until now, how these WD40 domain-containing proteins interact with Set1 and contribute to the stability of Set1 and H3K4 methylation has not been determined. In this study, we identified small basic and acidic patches that mediate protein interactions between the C terminus of Swd1 and the nSET domain of Set1. Absence of either the basic or acidic patches of Set1 and Swd1, respectively, disrupts the interaction between Set1 and Swd1, diminishes Set1 protein levels, and abolishes H3K4 methylation. Moreover, these basic and acidic patches are also important for cell growth, telomere silencing, and gene expression. We also show that the basic and acidic patches of Set1 and Swd1 are conserved in their human counterparts SET1A/B and RBBP5, respectively, and are needed for the protein interaction between SET1A and RBBP5. Therefore, this charge-based interaction is likely important for maintaining the protein stability of the human SET1A/B methyltransferase complexes so that proper H3K4 methylation, cell growth, and gene expression can also occur in mammals.
    Document Type:
    Reference
    Product Catalog Number:
    Multiple
    Product Catalog Name:
    Multiple

  • Modulating cell adhesion and spreading by control of FnIII7-10 orientation on charged self-assembled monolayers (SAMs) of alkanethiolates. 16514600

    In this work, we demonstrate that surface charge can be used to modulate cell adhesion/spreading through the control of the orientation of adsorbed FnIII(7-10), which is a cell-adhesive protein containing RGD residues. Carboxylic acid (COOH) and amine (NH(2))-terminated self-assembled monolayers (SAMs) of alkanethiolates were used as model negatively and positively charged surfaces, respectively. The adsorbed amount of FnIII(7-10) is controlled to be equivalent on both SAMs as confirmed by the adsorption isotherms determined using I(125)-radiolabeled FnIII(7-10.) The binding of a monoclonal antibody specific for the cell-binding domain of FnIII(7-10) was measured by surface plasmon resonance (SPR) to evaluate FnIII(7-10) orientations on different SAMs. Results indicate that adsorbed FnIII(7-10) on NH(2)-SAM has an orientation with more cell-binding domains accessible than on COOH-SAM, confirming our predictions from Monte Carlo simulations. Both phase contrast images and Vybrant MTT cell proliferation assays show that the adhesion/spreading of bovine aortic endothelial cells (BAECs) on the NH(2)-SAM is significantly better than that on the COOH-SAM coated with an equivalent amount of FnIII(7-10). These results indicate that surface charge can be used to specifically orient cell adhesive proteins such as FnIII(7-10), thus providing a promising strategy to increase the activity of materials incorporating biological moieties.
    Document Type:
    Reference
    Product Catalog Number:
    MAB1934
    Product Catalog Name:
    Anti-Fibronectin Antibody, cell binding peptide, clone 784A2A6 - (Anti-Fibronectin Antibody, cell binding peptide, clone 784A2A6)

  • Charge Durapore Cartridge C7SA98300

    Document Type:
    Certificate of Quality
    Lot Number:
    C7SA98300
    Product Catalog Number:
    CCGL73TP1
    Product Catalog Name:
    Charged Durapore® Cartridge 30 in. 0.22 µm Code 7 - (Charged Durapore® Cartridge 30 in. 0.22 µm Code 7)

  • Charge Durapore Cartridge C7NA78981

    Document Type:
    Certificate of Quality
    Lot Number:
    C7NA78981
    Product Catalog Number:
    CCGL73TP1
    Product Catalog Name:
    Charged Durapore® Cartridge 30 in. 0.22 µm Code 7 - (Charged Durapore® Cartridge 30 in. 0.22 µm Code 7)

  • Charge Durapore Cartridge C7SA08678

    Document Type:
    Certificate of Quality
    Lot Number:
    C7SA08678
    Product Catalog Number:
    CCGL01TP1
    Product Catalog Name:
    Charged Durapore® Cartridge 10 in. 0.22 µm Code 0 - (Charged Durapore® Cartridge 10 in. 0.22 µm Code 0)

  • Charge Durapore Cartridge C7PA87769

    Document Type:
    Certificate of Quality
    Lot Number:
    C7PA87769
    Product Catalog Number:
    CCGL71TP1
    Product Catalog Name:
    Charged Durapore® Cartridge 10 in. 0.22 µm Code 7 - (Charged Durapore® Cartridge 10 in. 0.22 µm Code 7)

  • Charge Durapore Cartridge C4DB71437

    Document Type:
    Certificate of Quality
    Lot Number:
    C4DB71437
    Product Catalog Number:
    CCGL71TP1
    Product Catalog Name:
    Charged Durapore® Cartridge 10 in. 0.22 µm Code 7 - (Charged Durapore® Cartridge 10 in. 0.22 µm Code 7)

  • Charge Durapore Cartridge C7PA92366

    Document Type:
    Certificate of Quality
    Lot Number:
    C7PA92366
    Product Catalog Number:
    CCGL01TP1
    Product Catalog Name:
    Charged Durapore® Cartridge 10 in. 0.22 µm Code 0 - (Charged Durapore® Cartridge 10 in. 0.22 µm Code 0)

  • Recognition of benztropine by the dopamine transporter (DAT) differs from that of the classical dopamine uptake inhibitors cocaine, methylphenidate, and mazindol as a fun ... 15879005

    Binding of cocaine to the dopamine transporter (DAT) protein blocks synaptic dopamine clearance, triggering the psychoactive effects associated with the drug; the discrete drug-protein interactions, however, remain poorly understood. A longstanding postulate holds that cocaine inhibits DAT-mediated dopamine transport via competition with dopamine for formation of an ionic bond with the DAT transmembrane aspartic acid residue D79. In the present study, DAT mutations of this residue were generated and assayed for translocation of radiolabeled dopamine and binding of radiolabeled DAT inhibitors under identical conditions. When feasible, dopamine uptake inhibition potency and apparent binding affinity K(i) values were determined for structurally diverse DAT inhibitors. The glutamic acid substitution mutant (D79E) displayed values indistinguishable from wild-type DAT in both assays for the charge-neutral cocaine analog 8-oxa-norcocaine, a finding not supportive of the D79 "salt bridge" ligand-docking model. In addressing whether the D79 side chain contributes to the DAT binding sites of other portions of the cocaine pharmacophore, only inhibitors with modifications of the tropane ring C-3 substituent, i.e., benztropine and its analogs, displayed a substantially altered dopamine uptake inhibition potency as a function of the D79E mutation. A single conservative amino acid substitution thus differentiated structural requirements for benztropine function relative to those for all other classical DAT inhibitors. Distinguishing the precise mechanism of action of this DAT inhibitor with relatively low abuse liability from that of cocaine may be attainable using DAT mutagenesis and other structure-function studies, opening the door to rational design of therapeutic agents for cocaine abuse.
    Document Type:
    Reference
    Product Catalog Number:
    MAB369
    Product Catalog Name:
    Anti-Dopamine Transporter Antibody, NT, clone DAT-Nt - (Anti-Dopamine Transporter Antibody, NT, clone DAT-Nt)