Mutational analysis of protein solubility enhancement using short peptide tags

Biopolymers ◽  
2007 ◽  
Vol 85 (1) ◽  
pp. 12-18 ◽  
Author(s):  
Atsushi Kato ◽  
Kosuke Maki ◽  
Teppei Ebina ◽  
Kunihiro Kuwajima ◽  
Kunitsugu Soda ◽  
...  
Keyword(s):  
Mutational Analysis ◽  
Protein Solubility ◽  
Solubility Enhancement ◽  
Short Peptide ◽  
Peptide Tags

Analysis and Control of Protein Crystallization Using Short Peptide Tags That Change Solubility without Affecting Structure, Thermal Stability, and Function

2015 ◽  
Vol 15 (6) ◽  
pp. 2703-2711 ◽  
Author(s):  
Mohammad Monirul Islam ◽  
Shigeyoshi Nakamura ◽  
Keiichi Noguchi ◽  
Masafumi Yohda ◽  
Shun-ichi Kidokoro ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Protein Crystallization ◽  
Short Peptide ◽  
Peptide Tags ◽  
And Function ◽  
And Control

Genetically Encoded Short Peptide Tags for Orthogonal Protein Labeling by Sfp and AcpS Phosphopantetheinyl Transferases

2007 ◽  
Vol 2 (5) ◽  
pp. 337-346 ◽  
Author(s):  
Zhe Zhou ◽  
Pablo Cironi ◽  
Alison J. Lin ◽  
Yangqing Xu ◽  
Siniša Hrvatin ◽  
...  
Keyword(s):  
Protein Labeling ◽  
Short Peptide ◽  
Peptide Tags ◽  
Phosphopantetheinyl Transferases

Short peptide tags increase the yield of C-terminally labeled protein

2007 ◽  
Vol 29 (7) ◽  
pp. 1065-1073 ◽  
Author(s):  
Teruaki Kobayashi ◽  
Miwa Shiratori ◽  
Hirofumi Nakano ◽  
Chikashi Eguchi ◽  
Makoto Shirai ◽  
...  
Keyword(s):  
Short Peptide ◽  
Peptide Tags

Detecting ligand-protein interactions inside cells using reactive peptide tags and split luciferase

2021 ◽  
Author(s):  
Tsuyoshi Takahashi ◽  
Hiroaki Hagiwara
Keyword(s):  
Protein Interactions ◽  
Short Peptide ◽  
Nanoluc Luciferase ◽  
Peptide Tags ◽  
Split Luciferase

We report a method for detecting ligand-protein interactions occurring within cells using short peptide reactive tags appended to ligands and proteins, along with a split NanoLuc luciferase. This method can...

scholarly journals Inactivation of Three RG(S/T)GR Pentapeptide-Containing Negative Regulators of HetR Results in Lethal Differentiation of Anabaena PCC 7120

Life ◽  
2020 ◽  
Vol 10 (12) ◽  
pp. 326
Author(s):  
Ivan Khudyakov ◽  
Grigory Gladkov ◽  
Jeff Elhai
Keyword(s):  
Mutational Analysis ◽  
Filamentous Cyanobacterium ◽  
Intercellular Signaling ◽  
Tight Control ◽  
Negative Regulators ◽  
Short Peptide ◽  
Anabaena Pcc 7120 ◽  
Cyanobacterium Anabaena ◽  
Anabaena Sp ◽  
Pcc 7120

The filamentous cyanobacterium Anabaena sp. PCC 7120 produces, during the differentiation of heterocysts, a short peptide PatS and a protein HetN, both containing an RGSGR pentapeptide essential for activity. Both act on the master regulator HetR to guide heterocyst pattern formation by controlling the binding of HetR to DNA and its turnover. A third small protein, PatX, with an RG(S/T)GR motif is present in all HetR-containing cyanobacteria. In a nitrogen-depleted medium, inactivation of patX does not produce a discernible change in phenotype, but its overexpression blocks heterocyst formation. Mutational analysis revealed that PatX is not required for normal intercellular signaling, but it nonetheless is required when PatS is absent to prevent rapid ectopic differentiation. Deprivation of all three negative regulators—PatS, PatX, and HetN—resulted in synchronous differentiation. However, in a nitrogen-containing medium, such deprivation leads to extensive fragmentation, cell lysis, and aberrant differentiation, while either PatX or PatS as the sole HetR regulator can establish and maintain a semiregular heterocyst pattern. These results suggest that tight control over HetR by PatS and PatX is needed to sustain vegetative growth and regulated development. The mutational analysis has been interpreted in light of the opposing roles of negative regulators of HetR and the positive regulator HetL.

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