Polycomb and polyhomeotic are constituents of a multimeric protein complex in chromatin of Drosophila melanogaster.

1992 ◽  
Vol 11 (8) ◽  
pp. 2941-2950 ◽  
Author(s):  
A. Franke ◽  
M. DeCamillis ◽  
D. Zink ◽  
N. Cheng ◽  
H.W. Brock ◽  
...  
2022 ◽  
Author(s):  
Ikuo Kurisaki ◽  
Shigenori Tanaka

The physicochemical entity of biological phenomenon in the cell is a network of biochemical reactions and the activity of such a network is regulated by multimeric protein complexes. Mass spectroscopy (MS) experiments and multimeric protein docking simulations based on structural bioinformatics techniques have revealed the molecular-level stoichiometry and static configuration of subcomplexes in their bound forms, then revealing the subcomplex populations and formation orders. Meanwhile, these methodologies are not designed to straightforwardly examine temporal dynamics of multimeric protein assembly and disassembly, essential physicochemical properties to understand functional expression mechanisms of proteins in the biological environment. To address the problem, we had developed an atomistic simulation in the framework of the hybrid Monte Carlo/Molecular Dynamics (hMC/MD) method and succeeded in observing disassembly of homomeric pentamer of the serum amyloid P component protein in experimentally consistent order. In this study, we improved the hMC/MD method to examine disassembly processes of the tryptophan synthase tetramer, a paradigmatic heteromeric protein complex in MS studies. We employed the likelihood-based selection scheme to determine a dissociation-prone subunit pair at each hMC/MD simulation cycle and achieved highly reliable predictions of the disassembly orders with the success rate over 0.9 without a priori knowledge of the MS experiments and structural bioinformatics simulations. We similarly succeeded in reliable predictions for the other three tetrameric protein complexes. These achievements indicate the potential availability of our hMC/MD approach as the general purpose methodology to obtain microscopic and physicochemical insights into multimeric protein complex formation.


2004 ◽  
Vol 72 (8) ◽  
pp. 4932-4932
Author(s):  
Daniel E. Voth ◽  
Maen Qa'Dan ◽  
Elaine E. Hamm ◽  
Joy M. Pelfrey ◽  
Jimmy D. Ballard

Author(s):  
Russell G. Foster ◽  
Leon Kreitzman

Circadian clocks in animals and plants arise from multiple and interconnected transcription–translation feedback loops that ensure the proper oscillation of thousands of genes in a tissue-specific manner. ‘The tick-tock of the molecular clock’ explains the transcription–translation feedback loop by describing the studies of circadian rhythms in Drosophila melanogaster, the fruit fly. The generation of a robust circadian rhythm entrained by the environment is achieved via multiple elements including the rate of transcription, translation, protein complex assembly, phosphorylation, other post-translation modification events, movement into the nucleus, transcriptional inhibition, and protein degradation. Similar mechanisms have been found in mammals, and insight is provided regarding research into how the mammalian molecular clock is entrained by light.


Author(s):  
Michael M. Morgan ◽  
MacDonald J. Christie ◽  
Thomas Steckler ◽  
Ben J. Harrison ◽  
Christos Pantelis ◽  
...  

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