scholarly journals 41. GNRH and TRH receptors: monitoring the formation of dynamic protein complexes in living cells

2003 ◽  
Vol 15 (9) ◽  
pp. 41
Author(s):  
K. A. Eidne
Keyword(s):  
Protein Complexes ◽  
Living Cells ◽  
Trh Receptors

scholarly journals Target Gene Specificity of E2F and Pocket Protein Family Members in Living Cells

2000 ◽  
Vol 20 (16) ◽  
pp. 5797-5807 ◽  
Author(s):  
Julie Wells ◽  
Kathryn E. Boyd ◽  
Christopher J. Fry ◽  
Stephanie M. Bartley ◽  
Peggy J. Farnham
Keyword(s):  
Cell Cycle ◽  
Target Gene ◽  
Target Genes ◽  
Protein Complexes ◽  
Current Model ◽  
Family Members ◽  
Living Cells ◽  
Gene Promoters ◽  
Pocket Protein ◽  
Protein Dna Interactions

ABSTRACT E2F-mediated transcription is thought to involve binding of an E2F-pocket protein complex to promoters in the G0 phase of the cell cycle and release of the pocket protein in late G1, followed by release of E2F in S phase. We have tested this model by monitoring protein-DNA interactions in living cells using a formaldehyde cross-linking and immunoprecipitation assay. We find that E2F target genes are bound by distinct E2F-pocket protein complexes which change as cells progress through the cell cycle. We also find that certain E2F target gene promoters are bound by pocket proteins when such promoters are transcriptionally active. Our data indicate that the current model applies only to certain E2F target genes and suggest that Rb family members may regulate transcription in both G0 and S phases. Finally, we find that a given promoter can be bound by one of several different E2F-pocket protein complexes at a given time in the cell cycle, suggesting that cell cycle-regulated transcription is a stochastic, not a predetermined, process.

Homomeric protein complexes: evolution and assembly

2010 ◽  
Vol 38 (4) ◽  
pp. 879-882 ◽  
Author(s):  
A.J. Venkatakrishnan ◽  
Emmanuel D. Levy ◽  
Sarah A. Teichmann
Keyword(s):  
Present Article ◽  
Protein Complexes ◽  
Living Cells ◽  
Current Understanding ◽  
Oligomeric Protein

Homo-oligomeric protein complexes are functionally vital and highly abundant in living cells. In the present article, we review our current understanding of their geometry and evolution, including aspects of the symmetry of these complexes and their interaction interfaces. Also, we briefly discuss the pathway of their assembly in solution.

scholarly journals Mass spectrometry-based methods for analysing the mitochondrial interactome in mammalian cells

2019 ◽  
Vol 167 (3) ◽  
pp. 225-231 ◽  
Author(s):  
Takumi Koshiba ◽  
Hidetaka Kosako
Keyword(s):  
Mass Spectrometry ◽  
Protein Interactions ◽  
Mammalian Cells ◽  
Protein Complexes ◽  
Living Cells ◽  
Protein Protein Interactions ◽  
Cellular Functions ◽  
Protein Protein Interaction ◽  
Membrane Protein Complexes ◽  
Protein Protein Interaction Networks

Abstract Protein–protein interactions are essential biologic processes that occur at inter- and intracellular levels. To gain insight into the various complex cellular functions of these interactions, it is necessary to assess them under physiologic conditions. Recent advances in various proteomic technologies allow to investigate protein–protein interaction networks in living cells. The combination of proximity-dependent labelling and chemical cross-linking will greatly enhance our understanding of multi-protein complexes that are difficult to prepare, such as organelle-bound membrane proteins. In this review, we describe our current understanding of mass spectrometry-based proteomics mapping methods for elucidating organelle-bound membrane protein complexes in living cells, with a focus on protein–protein interactions in mitochondrial subcellular compartments.

scholarly journals Revealing Structural Features and Affinities of Protein Complexes in Living Cells by MFIS-FRET

2016 ◽  
Vol 110 (3) ◽  
pp. 491a
Author(s):  
Qijun Ma ◽  
Marc Somssich ◽  
Stanislav Kalinin ◽  
Thomas Peulen ◽  
Ralf Kühnemuth ◽  
...  
Keyword(s):  
Protein Complexes ◽  
Structural Features ◽  
Living Cells

The denaturation of lipid-protein complexes as a cause of damage by freezing

1957 ◽  
Vol 147 (929) ◽  
pp. 427-433 ◽  
Keyword(s):  
Crystal Growth ◽  
Protein Complexes ◽  
Direct Consequence ◽  
Living Cells ◽  
Ice Crystals ◽  
Ice Crystal ◽  
Freezing Damage ◽  
Biological Origin ◽  
General Utility ◽  
Harmful Effects

The practice of cold storage for preserving labile material of biological origin is widespread. The general utility of this method and the successful preservation of living cells and tissues in the frozen state has overshadowed the fact that freezing can be a harmful process to living cells (Wood 1956). It used to be thought that the crushing or spearing action of ice crystal growth was the principal source of damage by freezing; indeed so reasonable is this theory that it is difficult to believe that some at least of the harmful effects of freezing are not due to this cause. The development of the theories of damage by ice crystal growth have been described in detail by Luyet & Gehenio (1940), and by Meryman (1956). By contrast with damage on a macroscopic scale which might occur during the growth of ice crystals there is evidence to show that freezing can damage the molecular constituents of living cells, and this is most unlikely to be a direct consequence of the intrusion of ice crystals. This aspect of the problem of freezing damage forms the basis of this paper.

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