scholarly journals Protein-based asymmetry and protein-protein interactions in FLP recombinase-mediated site-specific recombination.

1990 ◽  
Vol 265 (35) ◽  
pp. 21779-21788 ◽  
Author(s):  
X H Qian ◽  
R B Inman ◽  
M M Cox
Keyword(s):  
Protein Interactions ◽  
Protein Protein Interactions ◽  
Site Specific ◽  
Site Specific Recombination ◽  
Flp Recombinase

scholarly journals The Amino Terminus of Bacteriophage λ Integrase Is Involved in Protein-Protein Interactions during Recombination

2000 ◽  
Vol 182 (4) ◽  
pp. 1024-1034 ◽  
Author(s):  
Lea Jessop ◽  
Troy Bankhead ◽  
David Wong ◽  
Anca M. Segall
Keyword(s):  
Protein Interactions ◽  
Protein Protein Interactions ◽  
Site Specific ◽  
Site Specific Recombination ◽  
Amino Terminal ◽  
Terminal Domain ◽  
Protein Dna Interactions ◽  
Bacteriophage Lambda Integrase ◽  
Amino Terminal Domain ◽  
Genetic Assay

ABSTRACT Bacteriophage lambda integrase (Int) catalyzes at least four site-specific recombination pathways between pairs of attachment (att) sites. Protein-protein contacts between monomers of Int are presumed to be important for these site-specific recombination events for several reasons: Int binds to the att sites cooperatively, catalytic Int mutants can complement each other for strand cleavage, and crystal structures for two other recombinases in the Int family (Cre from phage P1 and Int from Haemophilus influenzae phage HP1) show extensive protein-protein contacts between monomers. We have begun to investigate interactions between Int monomers by three approaches. First, using a genetic assay, we show that regions of protein-protein interactions occur throughout Int, including in the amino-terminal domain. This domain was previously thought to be important only for high-affinity protein-DNA interactions. Second, we have found that an amino-terminal His tag reduces cooperative binding to DNA. This disruption in cooperativity decreases the stable interaction of Int with core sites, where catalysis occurs. Third, using protein-protein cross-linking to investigate the multimerization of Int during recombination, we show that Int predominantly forms dimers, trimers, and tetramers. Moreover, we show that the cysteine at position 25 is present at or near the interface between monomers that is involved in the formation of dimers and tetramers. Our evidence indicates that the amino-terminal domain of Int is involved in protein-protein interactions that are likely to be important for recombination.

Protein-protein interactions in a higher-order structure direct lambda site-specific recombination

1987 ◽  
Vol 195 (3) ◽  
pp. 481-493 ◽  
Author(s):  
John F. Thompson ◽  
Lina Moitoso de Vargas ◽  
Sarah E. Skinner ◽  
Arthur Landy
Keyword(s):  
Protein Interactions ◽  
Higher Order ◽  
Order Structure ◽  
Protein Protein Interactions ◽  
Site Specific ◽  
Site Specific Recombination

Engineering an acetyllysine reader with photocrosslinking amino acid for interactome profiling

2021 ◽  
Author(s):  
Babu Sudhamalla ◽  
Anirban Roy ◽  
Soumen Barman ◽  
Jyotirmayee Padhan
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Interactions ◽  
Unnatural Amino Acids ◽  
Protein Protein Interactions ◽  
Site Specific ◽  
Powerful Approach

The site-specific installation of light-activable crosslinker unnatural amino acids offers a powerful approach to trap transient protein-protein interactions both in vitro and in vivo. Herein, we engineer a bromodomain to...

Furan warheads for covalent trapping of weak protein-protein interactions: cross-linking of thymosin β4 to actin

2021 ◽  
Author(s):  
Laia Miret Casals ◽  
Willem Vannecke ◽  
Kurt Hoogewijs ◽  
Gianluca Arauz ◽  
Marina Gay ◽  
...  
Keyword(s):  
Protein Interaction ◽  
Protein Interactions ◽  
3D Structure ◽  
Cross Linking ◽  
Thymosin Β4 ◽  
Protein Protein Interactions ◽  
Site Specific ◽  
Protein Protein Interaction ◽  
Covalent Trapping

We describe furan as a triggerable ‘warhead’ for site-specific cross-linking using the actin and thymosin β4 (Tβ4)-complex as model of a weak and dynamic protein-protein interaction with known 3D structure...

scholarly journals Engineering bromodomains with a photoactive amino acid by engaging ‘Privileged’ tRNA synthetases

2020 ◽  
Vol 56 (25) ◽  
pp. 3641-3644
Author(s):  
Shana Wagner ◽  
Babu Sudhamalla ◽  
Philip Mannes ◽  
Sushma Sappa ◽  
Sam Kavoosi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Chemical Synthesis ◽  
Protein Interactions ◽  
Protein Protein Interactions ◽  
Site Specific ◽  
Trna Synthetases

An improved chemical synthesis, site-specific incorporation and enhanced photo-crosslinking ability of tmdF have been demonstrated in the context of protein–protein interactions.

FLP recombinase-mediated site-specific recombination in rice

2008 ◽  
Vol 6 (2) ◽  
pp. 176-188 ◽  
Author(s):  
Qian Hu ◽  
Halina Kononowicz-Hodges ◽  
Kimberly Nelson-Vasilchik ◽  
David Viola ◽  
Peiyu Zeng ◽  
...  
Keyword(s):  
Site Specific ◽  
Site Specific Recombination ◽  
Flp Recombinase

scholarly journals Site-specific glycosylation regulates the form and function of the intermediate filament cytoskeleton

eLife ◽  
2018 ◽  
Vol 7 ◽  
Author(s):  
Heather J Tarbet ◽  
Lee Dolat ◽  
Timothy J Smith ◽  
Brett M Condon ◽  
E Timothy O'Brien ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Transferase Activity ◽  
Protein Protein Interactions ◽  
Site Specific ◽  
Form And Function ◽  
Glycosylation Sites ◽  
Wide Range ◽  
Dynamics And Function ◽  
Glcnac Transferase ◽  
And Function

Intermediate filaments (IF) are a major component of the metazoan cytoskeleton and are essential for normal cell morphology, motility, and signal transduction. Dysregulation of IFs causes a wide range of human diseases, including skin disorders, cardiomyopathies, lipodystrophy, and neuropathy. Despite this pathophysiological significance, how cells regulate IF structure, dynamics, and function remains poorly understood. Here, we show that site-specific modification of the prototypical IF protein vimentin with O-linked β-N-acetylglucosamine (O-GlcNAc) mediates its homotypic protein-protein interactions and is required in human cells for IF morphology and cell migration. In addition, we show that the intracellular pathogen Chlamydia trachomatis, which remodels the host IF cytoskeleton during infection, requires specific vimentin glycosylation sites and O-GlcNAc transferase activity to maintain its replicative niche. Our results provide new insight into the biochemical and cell biological functions of vimentin O-GlcNAcylation, and may have broad implications for our understanding of the regulation of IF proteins in general.

Sign in / Sign up

Export Citation Format

Share Document