scholarly journals The transmission of stability or instability from site specific protein-DNA complexes

1977 ◽  
Vol 4 (8) ◽  
pp. 2779-2797 ◽  
Author(s):  
Roger M. Wartell
Keyword(s):  
Specific Protein ◽  
Dna Complexes ◽  
Site Specific

Role of the hydrophobic effect in stability of site-specific protein-DNA complexes

1989 ◽  
Vol 209 (4) ◽  
pp. 801-816 ◽  
Author(s):  
Jeung-Hoi Ha ◽  
Ruth S. Spolar ◽  
M.Thomas Record
Keyword(s):  
Hydrophobic Effect ◽  
Specific Protein ◽  
Dna Complexes ◽  
Site Specific

scholarly journals The PCNA unloader Elg1 promotes recombination at collapsed replication forks in fission yeast

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Sanjeeta Tamang ◽  
Anastasiya Kishkevich ◽  
Carl A Morrow ◽  
Fekret Osman ◽  
Manisha Jalan ◽  
...  
Keyword(s):  
Homologous Recombination ◽  
Replication Fork ◽  
Specific Protein ◽  
Replication Forks ◽  
Dna Complexes ◽  
Site Specific ◽  
Dna Helicases ◽  
Sliding Clamp ◽  
Recombination Proteins ◽  
Stalled Fork

Protein-DNA complexes can impede DNA replication and cause replication fork collapse. Whilst it is known that homologous recombination is deployed in such instances to restart replication, it is unclear how a stalled fork transitions into a collapsed fork at which recombination proteins can load. Previously we established assays in Schizosaccharomyces pombe for studying recombination induced by replication fork collapse at the site-specific protein-DNA barrier RTS1 (Nguyen et al., 2015). Here, we provide evidence that efficient recruitment/retention of two key recombination proteins (Rad51 and Rad52) to RTS1 depends on unloading of the polymerase sliding clamp PCNA from DNA by Elg1. We also show that, in the absence of Elg1, reduced recombination is partially suppressed by deleting fbh1 or, to a lesser extent, srs2, which encode known anti-recombinogenic DNA helicases. These findings suggest that PCNA unloading by Elg1 is necessary to limit Fbh1 and Srs2 activity, and thereby enable recombination to proceed.

Systematic Engineering of a Protein Nanocage for High-Yield, Site-Specific Modification

2018 ◽  
Author(s):  
Daniel D. Brauer ◽  
Emily C. Hartman ◽  
Daniel L.V. Bader ◽  
Zoe N. Merz ◽  
Danielle Tullman-Ercek ◽  
...  
Keyword(s):  
Small Molecules ◽  
Protein Modification ◽  
Positive Charge ◽  
Specific Protein ◽  
High Yield ◽  
Site Specific ◽  
Protein Cage ◽  
Protein Carriers ◽  
Site Selective ◽  
Targeted Library

<div> <p>Site-specific protein modification is a widely-used strategy to attach drugs, imaging agents, or other useful small molecules to protein carriers. N-terminal modification is particularly useful as a high-yielding, site-selective modification strategy that can be compatible with a wide array of proteins. However, this modification strategy is incompatible with proteins with buried or sterically-hindered N termini, such as virus-like particles like the well-studied MS2 bacteriophage coat protein. To assess VLPs with improved compatibility with these techniques, we generated a targeted library based on the MS2-derived protein cage with N-terminal proline residues followed by three variable positions. We subjected the library to assembly, heat, and chemical selections, and we identified variants that were modified in high yield with no reduction in thermostability. Positive charge adjacent to the native N terminus is surprisingly beneficial for successful extension, and over 50% of the highest performing variants contained positive charge at this position. Taken together, these studies described nonintuitive design rules governing N-terminal extensions and identified successful extensions with high modification potential.</p> </div>

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