Cargando…
Urea Unfolding Study of E. coli Alanyl-tRNA Synthetase and Its Monomeric Variants Proves the Role of C-Terminal Domain in Stability
E. coli alanyl-tRNA exists as a dimer in its native form and the C-terminal coiled-coil part plays an important role in the dimerization process. The truncated N-terminal containing the first 700 amino acids (1–700) forms a monomeric variant possessing similar aminoacylation activity like wild type....
Autores principales: | Banerjee, Baisakhi, Banerjee, Rajat |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi Publishing Corporation
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4649089/ https://www.ncbi.nlm.nih.gov/pubmed/26617997 http://dx.doi.org/10.1155/2015/805681 |
Ejemplares similares
-
Lysine Acetylation Regulates Alanyl-tRNA Synthetase Activity in Escherichia coli
por: Umehara, Takuya, et al.
Publicado: (2018) -
Impact of alanyl-tRNA synthetase editing deficiency in yeast
por: Zhang, Hong, et al.
Publicado: (2021) -
A naturally occurring mini-alanyl-tRNA synthetase
por: Antika, Titi Rindi, et al.
Publicado: (2023) -
Alanyl-tRNA Synthetase Quality Control Prevents Global Dysregulation of the Escherichia coli Proteome
por: Kelly, Paul, et al.
Publicado: (2019) -
Novel Alanyl-tRNA Synthetase 2 Pathogenic Variants in Leukodystrophies
por: Wang, Xingao, et al.
Publicado: (2019)