Identification of Gal4 activation domain-binding proteins in the 26S proteasome by periodate-triggered cross-linking

2005 ◽  
Vol 1 (5-6) ◽  
pp. 366 ◽  
Author(s):  
Chase T. Archer ◽  
Lyle Burdine ◽  
Thomas Kodadek
Keyword(s):  
Binding Proteins ◽  
26S Proteasome ◽  
Cross Linking ◽  
Activation Domain ◽  
Gal4 Activation Domain

scholarly journals Identification through chemical cross-linking of distinct granulocyte- macrophage colony-stimulating factor and interleukin-3 receptors on myeloid leukemic cells, KG-1

Blood ◽  
1989 ◽  
Vol 74 (8) ◽  
pp. 2652-2656 ◽  
Author(s):  
T Gesner ◽  
RA Mufson ◽  
KJ Turner ◽  
SC Clark
Keyword(s):  
Binding Proteins ◽  
Myelogenous Leukemia ◽  
Cross Linking ◽  
Colony Stimulating Factor ◽  
Interleukin 3 ◽  
Gm Csf ◽  
Macrophage Colony Stimulating Factor ◽  
Macrophage Colony ◽  
Stimulating Factor ◽  
Chemical Cross Linking

Abstract Granulocyte/macrophage colony-stimulating factor (GM-CSF) and interleukin-3 (IL-3) each bind specifically to a small number of high- affinity receptors present on the surface of the cells of the acute myelogenous leukemia line, KG-1. Through chemical cross-linking of IL-3 and GM-CSF to KG-1 cells, we identified distinct binding proteins for each of these cytokines with approximate molecular masses of 69 and 93 Kd, respectively. Although these two binding proteins are distinct, GM- CSF and IL-3 compete with each other for binding to KG-1 cells. Other cell lines, which express receptors for either factor but not for both do not display this cross-competition for binding with IL-3 and GM-CSF. These findings imply that distinct IL-3 and GM-CSF binding proteins are expressed on the cell surface and that an association exists between these proteins on KG-1 cells.

scholarly journals Biochemical Characterization of the TATA-binding Protein-Gal4 Activation Domain Complex

2000 ◽  
Vol 275 (41) ◽  
pp. 31914-31920 ◽  
Author(s):  
Yueqing Xie ◽  
Carilee Denison ◽  
Sang-Hwa Yang ◽  
David A. Fancy ◽  
Thomas Kodadek
Keyword(s):  
Biochemical Characterization ◽  
Binding Protein ◽  
Tata Binding Protein ◽  
Activation Domain ◽  
Gal4 Activation Domain

scholarly journals Assembly of the Drosophila 26 S proteasome is accompanied by extensive subunit rearrangements

2002 ◽  
Vol 365 (2) ◽  
pp. 527-536 ◽  
Author(s):  
Éva KURUCZ ◽  
István ANDÓ ◽  
Máté SÜMEGI ◽  
Harald HÖLZL ◽  
Barbara KAPELARI ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
26S Proteasome ◽  
Cross Linking ◽  
20S Proteasome ◽  
Electron Microscopic ◽  
Immunoblot Assay ◽  
Optimal Conformation ◽  
Regulatory Complex ◽  
Atpase Subunits ◽  
The Cross

The subunit contacts in the regulatory complex of the Drosophila 26 S proteasome were studied through the cross-linking of closely spaced subunits of the complex, and analysis of the cross-linking pattern in an immunoblot assay with the use of subunit-specific monoclonal antibodies. The cross-linking pattern of the purified 26 S proteasome exhibits significant differences as compared with that of the purified free regulatory complex. It is shown that the observed differences are due to extensive rearrangement of the subunit contacts accompanying the assembly of the 26 S proteasome from the regulatory complex and the 20S proteasome. Cross-linking studies and electron microscopic examinations revealed that these changes are reversible and follow the assembly or the disassembly of the 26 S proteasome. Although the majority of the changes observed in the subunit contacts affected the hexameric ring of the ATPase subunits, the alterations extended over the whole of the regulatory complex, affecting subunit contacts even in the lid subcomplex. Changes in the subunit contacts, similar to those in the regulatory complex, were detected in the 20S proteasome. These observations indicate that the assembly of the 26 S proteasome is not simply a passive docking of two rigid subcomplexes. In the course of the assembly, the interacting subcomplexes mutually rearrange their structures so as to create the optimal conformation required for the assembly and the proper functioning of the 26S proteasome.

Novel Photo Affinity Cross-linking Resin for the Isolation of Heparin Binding Proteins

2000 ◽  
Vol 15 (6) ◽  
pp. 468-477 ◽  
Author(s):  
YASUO SUDA ◽  
MEGUMI NAKAMURA ◽  
SHUHEI KOSHIDA ◽  
SHOICHI KUSUMOTO ◽  
MICHAEL SOBEL
Keyword(s):  
Binding Proteins ◽  
Cross Linking ◽  
Heparin Binding

[43] Ultraviolet cross-linking of DNA binding proteins

1995 ◽  
pp. 632-641 ◽  
Author(s):  
Shigeki Miyamoto ◽  
Keith Cauley ◽  
Inder M. Verma
Keyword(s):  
Dna Binding ◽  
Binding Proteins ◽  
Dna Binding Proteins ◽  
Cross Linking

scholarly journals New Cephamycin Antibiotic, CS-1170: Binding Affinity to Penicillin-Binding Proteins and Inhibition of Peptidoglycan Cross-Linking Reactions in Escherichia coli

1978 ◽  
Vol 14 (5) ◽  
pp. 780-785 ◽  
Author(s):  
S. Ohya ◽  
M. Yamazaki ◽  
S. Sugawara ◽  
S. Tamaki ◽  
M. Matsuhashi
Keyword(s):  
Escherichia Coli ◽  
Binding Affinity ◽  
Binding Proteins ◽  
Cross Linking ◽  
Penicillin Binding Proteins

scholarly journals Actin Cross-Linking Toxin Is a Universal Inhibitor of Tandem-Organized and Oligomeric G-Actin Binding Proteins

2018 ◽  
Vol 28 (10) ◽  
pp. 1536-1547.e9 ◽  
Author(s):  
Elena Kudryashova ◽  
David B. Heisler ◽  
Blake Williams ◽  
Alyssa J. Harker ◽  
Kyle Shafer ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Actin Binding ◽  
Cross Linking ◽  
Actin Binding Proteins

Identification of SUMO Binding Proteins Enriched after Covalent Photo-Cross-Linking

2020 ◽  
Vol 15 (9) ◽  
pp. 2406-2414 ◽  
Author(s):  
Kira Brüninghoff ◽  
Annika Aust ◽  
Kim F. Taupitz ◽  
Stephanie Wulff ◽  
Wolfgang Dörner ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Cross Linking ◽  
Sumo Binding Proteins
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