A ubiquitous disordered protein interaction module orchestrates transcription elongation

Science ◽  
2021 ◽  
Vol 374 (6571) ◽  
pp. 1113-1121
Author(s):  
Katerina Cermakova ◽  
Jonas Demeulemeester ◽  
Vanda Lux ◽  
Monika Nedomova ◽  
Seth R. Goldman ◽  
...  
Keyword(s):  
Protein Interaction ◽  
Transcription Elongation ◽  
Disordered Protein

scholarly journals Interactome-wide prediction of short, disordered protein interaction motifs in humans

2012 ◽  
Vol 8 (1) ◽  
pp. 282-295 ◽  
Author(s):  
Richard J. Edwards ◽  
Norman E. Davey ◽  
Kevin O' Brien ◽  
Denis C. Shields
Keyword(s):  
Protein Interaction ◽  
Disordered Protein

Linking transcription, RNA polymerase II elongation and alternative splicing

2020 ◽  
Vol 477 (16) ◽  
pp. 3091-3104 ◽  
Author(s):  
Luciana E. Giono ◽  
Alberto R. Kornblihtt
Keyword(s):  
Gene Expression ◽  
Alternative Splicing ◽  
Rna Polymerase Ii ◽  
Environmental Changes ◽  
Transcription Elongation ◽  
Single Gene ◽  
Regulation Of Gene Expression ◽  
Regulation Of Transcription ◽  
Stepping Stones ◽  
Eukaryotic Transcription

Gene expression is an intricately regulated process that is at the basis of cell differentiation, the maintenance of cell identity and the cellular responses to environmental changes. Alternative splicing, the process by which multiple functionally distinct transcripts are generated from a single gene, is one of the main mechanisms that contribute to expand the coding capacity of genomes and help explain the level of complexity achieved by higher organisms. Eukaryotic transcription is subject to multiple layers of regulation both intrinsic — such as promoter structure — and dynamic, allowing the cell to respond to internal and external signals. Similarly, alternative splicing choices are affected by all of these aspects, mainly through the regulation of transcription elongation, making it a regulatory knob on a par with the regulation of gene expression levels. This review aims to recapitulate some of the history and stepping-stones that led to the paradigms held today about transcription and splicing regulation, with major focus on transcription elongation and its effect on alternative splicing.

Protein protein interaction of p53 and p73 with YY1 in human hepatocellular carcinoma

2011 ◽  
Vol 49 (01) ◽  
Author(s):  
LC Koenig ◽  
C Sandig ◽  
MH Bender ◽  
W Stremmel ◽  
M Müller-Schilling
Keyword(s):  
Hepatocellular Carcinoma ◽  
Protein Interaction ◽  
Human Hepatocellular Carcinoma ◽  
Protein Protein Interaction

0513 Effect of γ radiation on physicochemical properties, protein-protein interaction, and microstructure of whey proteins

2016 ◽  
Vol 94 (suppl_5) ◽  
pp. 246-246
Author(s):  
M. Guo ◽  
X. Wang ◽  
F. Lee ◽  
J. Lv ◽  
D. Zhang
Keyword(s):  
Physicochemical Properties ◽  
Protein Interaction ◽  
Whey Proteins ◽  
Γ Radiation ◽  
Protein Protein Interaction

Self-Assembling Micelles Based on an Intrinsically Disordered Protein Domain

2018 ◽  
Author(s):  
Sarah Klass ◽  
Matthew J. Smith ◽  
Tahoe Fiala ◽  
Jessica Lee ◽  
Anthony Omole ◽  
...  
Keyword(s):  
Drug Delivery ◽  
Fusion Proteins ◽  
Organic Molecules ◽  
Intrinsically Disordered Protein ◽  
Protein Domain ◽  
Enzymatic Cleavage ◽  
Intrinsically Disordered ◽  
Disordered Protein ◽  
Self Assembling ◽  
Protein Tag

Herein, we describe a new series of fusion proteins that have been developed to self-assemble spontaneously into stable micelles that are 27 nm in diameter after enzymatic cleavage of a solubilizing protein tag. The sequences of the proteins are based on a human intrinsically disordered protein, which has been appended with a hydrophobic segment. The micelles were found to form across a broad range of pH, ionic strength, and temperature conditions, with critical micelle concentration (CMC) values below 1 µM being observed in some cases. The reported micelles were found to solubilize hydrophobic metal complexes and organic molecules, suggesting their potential suitability for catalysis and drug delivery applications.

Sign in / Sign up

Export Citation Format

Share Document