Versatile and Efficient Site-Specific Protein Functionalization by Tubulin Tyrosine Ligase

2015 ◽  
Vol 54 (46) ◽  
pp. 13787-13791 ◽  
Author(s):  
Dominik Schumacher ◽  
Jonas Helma ◽  
Florian A. Mann ◽  
Garwin Pichler ◽  
Francesco Natale ◽  
...  
Keyword(s):  
Specific Protein ◽  
Site Specific ◽  
Tubulin Tyrosine Ligase ◽  
Protein Functionalization

scholarly journals Broad substrate tolerance of tubulin tyrosine ligase enables one-step site-specific enzymatic protein labeling

2017 ◽  
Vol 8 (5) ◽  
pp. 3471-3478 ◽  
Author(s):  
Dominik Schumacher ◽  
Oliver Lemke ◽  
Jonas Helma ◽  
Lena Gerszonowicz ◽  
Verena Waller ◽  
...  
Keyword(s):  
Protein Labeling ◽  
Site Specific ◽  
Wide Applicability ◽  
One Step ◽  
Tubulin Tyrosine Ligase ◽  
Protein Functionalization ◽  
Substrate Tolerance ◽  
Step Site

The broad substrate tolerance of tubulin tyrosine ligase enables its wide applicability for protein functionalization.

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>

scholarly journals Protein ubiquitination via dehydroalanine: development and insights into the diastereoselective 1,4-addition step

2016 ◽  
Vol 14 (21) ◽  
pp. 4817-4823 ◽  
Author(s):  
Roman Meledin ◽  
Sachitanand M. Mali ◽  
Sumeet K. Singh ◽  
Ashraf Brik
Keyword(s):  
Specific Protein ◽  
Site Specific ◽  
Isopeptide Bond ◽  
Protein Ubiquitination

We report a strategy for site-specific protein ubiquitination using dehydroalanine (Dha) chemistry for the preparation of ubiquitin conjugates bearing a very close mimic of the native isopeptide bond.

scholarly journals Peptide-tags for site-specific protein labelling in vitro and in vivo

2016 ◽  
Vol 12 (6) ◽  
pp. 1731-1745 ◽  
Author(s):  
Jonathan Lotze ◽  
Ulrike Reinhardt ◽  
Oliver Seitz ◽  
Annette G. Beck-Sickinger
Keyword(s):  
Metal Ions ◽  
Small Molecules ◽  
Protein Localization ◽  
Specific Protein ◽  
Site Specific ◽  
Protein Labelling ◽  
Peptide Interactions ◽  
Peptide Tags

Peptide-tag based labelling can be achieved by (i) enzymes (ii) recognition of metal ions or small molecules and (iii) peptide–peptide interactions and enables site-specific protein visualization to investigate protein localization and trafficking.

scholarly journals Site-specific Protein Dynamics in Communication Pathway from Sensor to Signaling Domain of Oxygen Sensor Protein, HemAT-Bs

2012 ◽  
Vol 287 (24) ◽  
pp. 19973-19984 ◽  
Author(s):  
Samir F. El-Mashtoly ◽  
Minoru Kubo ◽  
Yuzong Gu ◽  
Hitomi Sawai ◽  
Satoru Nakashima ◽  
...  
Keyword(s):  
Protein Dynamics ◽  
Oxygen Sensor ◽  
Specific Protein ◽  
Site Specific ◽  
Sensor Protein ◽  
Signaling Domain ◽  
Communication Pathway

scholarly journals Site specific protein O-glucosylation with bacterial toxins

2016 ◽  
Vol 52 (88) ◽  
pp. 13024-13026 ◽  
Author(s):  
Y. Sun ◽  
L. M. Willis ◽  
H. R. Batchelder ◽  
M. Nitz
Keyword(s):  
Kinetic Parameters ◽  
Specific Protein ◽  
Bacterial Toxins ◽  
Maldi Ms ◽  
Toxin B ◽  
Site Specific

Using a MALDI-MS based assay, the kinetic parameters for peptide glucosylation using the C. difficile toxin B glycosyltransferase domain were determined.

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