A Conserved Histidine Residue Drives Extein Dependence in an Enhanced Atypically Split Intein.
Journal
Journal of the American Chemical Society
ISSN: 1520-5126
Titre abrégé: J Am Chem Soc
Pays: United States
ID NLM: 7503056
Informations de publication
Date de publication:
19 10 2022
19 10 2022
Historique:
pubmed:
5
10
2022
medline:
21
10
2022
entrez:
4
10
2022
Statut:
ppublish
Résumé
Split intein-mediated protein trans-splicing (PTS) is widely applied in chemical biology and biotechnology to carry out traceless and specific protein ligation. However, the external residues immediately flanking the intein (exteins) can reduce the splicing rate, thereby limiting certain applications of PTS. Splicing by a recently developed intein with atypical split architecture ("Cat") exhibits a stark dependence on the sequence of its N-terminal extein residues. Here, we further developed Cat using error-prone polymerase chain reaction (PCR) and a cell-based selection assay to produce Cat*, which exhibits greatly enhanced PTS activity in the presence of unfavorable N-extein residues. We then applied solution nuclear magnetic resonance spectroscopy and molecular dynamics simulations to explore how the dynamics of a conserved B-block histidine residue (His
Identifiants
pubmed: 36194550
doi: 10.1021/jacs.2c08985
pmc: PMC10241006
mid: NIHMS1859971
doi:
Substances chimiques
Histidine
4QD397987E
Proteins
0
Types de publication
Journal Article
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
19196-19203Subventions
Organisme : NIH HHS
ID : S10 OD016305
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM086868
Pays : United States
Organisme : NIGMS NIH HHS
ID : P41 GM066354
Pays : United States
Organisme : NIGMS NIH HHS
ID : R37 GM086868
Pays : United States
Organisme : NCRR NIH HHS
ID : C06 RR017528
Pays : United States
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