Consequences of the Endogenous N-Glycosylation of Human Ribonuclease 1.


Journal

Biochemistry
ISSN: 1520-4995
Titre abrégé: Biochemistry
Pays: United States
ID NLM: 0370623

Informations de publication

Date de publication:
19 02 2019
Historique:
pubmed: 12 1 2019
medline: 27 11 2019
entrez: 12 1 2019
Statut: ppublish

Résumé

Ribonuclease 1 (RNase 1) is the most prevalent human homologue of the archetypal enzyme RNase A. RNase 1 contains sequons for N-linked glycosylation at Asn34, Asn76, and Asn88 and is N-glycosylated at all three sites in vivo. The effect of N-glycosylation on the structure and function of RNase 1 is unknown. By using an engineered strain of the yeast Pichia pastoris, we installed a heptasaccharide (Man

Identifiants

pubmed: 30633504
doi: 10.1021/acs.biochem.8b01246
pmc: PMC6380942
mid: NIHMS1008659
doi:

Substances chimiques

RNA, Double-Stranded 0
Recombinant Proteins 0
Asparagine 7006-34-0
Ribonuclease, Pancreatic EC 3.1.27.5

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

987-996

Subventions

Organisme : NCI NIH HHS
ID : R01 CA073808
Pays : United States

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Auteurs

Valerie T Ressler (VT)

Department of Chemistry , Massachusetts Institute of Technology , Cambridge , Massachusetts 02139 , United States.

Ronald T Raines (RT)

Department of Chemistry , Massachusetts Institute of Technology , Cambridge , Massachusetts 02139 , United States.

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Classifications MeSH