Einzeltreffer — DigiBib

Evolution shapes protein sequences for their functions. Here, we studied the moonlighting functions of the N-linked sequon NXS/T, where X is not P, in human nucleocytosolic proteins. By comparing membrane and secreted proteins in which sequons are well known for N-glycosylation, we discovered that cyto-sequons can participate in nucleic acid binding, particularly in zinc finger proteins. Our global studies further discovered that sequon occurrence is largely proportional to protein length. The contribution of sequons to protein functions, including both N-glycosylation and nucleic acid binding, can be regulated through their density as well as the biased usage between NXS and NXT. In proteins where other PTMs or structural features are rich, such as phosphorylation, transmembrane ɑ-helices, and disulfide bridges, sequon occurrence is scarce. The information acquired here should help understand the relationship between protein sequence and function and assist future protein design and engineering.

Titel:	A quest for cytosolic sequons and their functions.
Autor/in / Beteiligte Person:	Desai, M ; Chowdhury, SR ; Sun, B
Link:	Full Text Finder (Volltext)
Zeitschrift:	Scientific reports, Jg. 14 (2024-04-02), Heft 1, S. 7736
Veröffentlichung:	London : Nature Publishing Group, copyright 2011-, 2024
Medientyp:	academicJournal
ISSN:	2045-2322 (electronic)
DOI:	10.1038/s41598-024-57334-1
Schlagwort:	Humans Glycosylation Amino Acid Sequence Phosphorylation Proteins metabolism Nucleic Acids metabolism
Sonstiges:	Nachgewiesen in: MEDLINE Sprachen: English Publication Type: Journal Article Language: English [Sci Rep] 2024 Apr 02; Vol. 14 (1), pp. 7736. <i>Date of Electronic Publication: </i>2024 Apr 02. MeSH Terms: Proteins* / metabolism ; Nucleic Acids* / metabolism ; Humans ; Glycosylation ; Amino Acid Sequence ; Phosphorylation References: Nucleic Acids Res. 2022 Jul 5;50(W1):W216-W221. (PMID: 35325185) ; Mol Biol Evol. 2011 May;28(5):1565-8. (PMID: 21273632) ; Comput Biol Chem. 2011 Apr;35(2):57-61. (PMID: 21353643) ; Nucleic Acids Res. 2001 Jul 1;29(13):2860-74. (PMID: 11433033) ; Cell. 2009 Jan 23;136(2):272-83. (PMID: 19167329) ; Sci Rep. 2019 Nov 4;9(1):15975. (PMID: 31685900) ; Int J Mol Sci. 2023 Nov 10;24(22):. (PMID: 38003370) ; Cell. 2006 Sep 8;126(5):855-67. (PMID: 16959566) ; Proc Natl Acad Sci U S A. 2009 Aug 11;106(32):13421-6. (PMID: 19666543) ; Cell. 2006 Sep 8;126(5):841-5. (PMID: 16959563) ; Structure. 1996 Oct 15;4(10):1171-80. (PMID: 8939742) ; Biochim Biophys Acta. 1999 Dec 6;1473(1):4-8. (PMID: 10580125) ; PLoS One. 2016 Jul 06;11(7):e0158704. (PMID: 27384774) ; Proc Natl Acad Sci U S A. 2023 Jan 17;120(3):e2212501120. (PMID: 36634135) ; Genetics. 2011 Aug;188(4):773-82. (PMID: 21828278) ; PLoS One. 2013;8(1):e53785. (PMID: 23372670) ; Molecules. 2021 Dec 02;26(23):. (PMID: 34885895) ; Annu Rev Biochem. 2010;79:213-31. (PMID: 20192761) ; Trends Biotechnol. 2013 Jul;31(7):397-405. (PMID: 23664777) ; J Mol Biol. 1999 Mar 12;286(5):1651-62. (PMID: 10064721) ; Pac Symp Biocomput. 2002;:310-22. (PMID: 11928486) ; J Mol Biol. 1999 Mar 12;286(5):1633-49. (PMID: 10064720) ; Glycobiology. 2004 Feb;14(2):103-14. (PMID: 14514716) ; Science. 1991 May 10;252(5007):809-17. (PMID: 2028256) ; Int J Mol Sci. 2021 Jan 18;22(2):. (PMID: 33477647) ; Mol Biol Evol. 2002 Dec;19(12):2118-30. (PMID: 12446804) ; PLoS One. 2014 Jan 24;9(1):e86088. (PMID: 24475074) ; Cell. 2009 Dec 24;139(7):1229-41. (PMID: 20064370) ; Biochim Biophys Acta. 2005 Nov 15;1726(2):121-37. (PMID: 16126345) ; Nat Commun. 2014;5:3099. (PMID: 24434425) ; Protein Eng. 1990 Apr;3(5):433-42. (PMID: 2349213) ; Curr Opin Struct Biol. 2011 Oct;21(5):576-82. (PMID: 21978957) ; Biochem J. 1983 Feb 1;209(2):331-6. (PMID: 6847620) ; Nat Methods. 2009 Nov;6(11):786-7. (PMID: 19876014) ; Bioorg Med Chem. 1995 Dec;3(12):1565-78. (PMID: 8770382) ; Curr Opin Struct Biol. 2006 Oct;16(5):600-7. (PMID: 16938454) Contributed Indexing: Keywords: Asx turns; Membrane protein topology; N-glycosylation; Posttranslational modifications; Protein structure and function; Protein-DNA binding; Sequons; Transmembrane domains; Zinc finger proteins; β-turns Substance Nomenclature: 0 (Proteins) ; 0 (Nucleic Acids) Entry Date(s): Date Created: 20240402 Date Completed: 20240404 Latest Revision: 20240405 Update Code: 20240405 PubMed Central ID: PMC10987669

Klicken Sie ein Format an und speichern Sie dann die Daten oder geben Sie eine Empfänger-Adresse ein und lassen Sie sich per Email zusenden.

BibTeX Citavi, JabRef, u.a.
(Literaturverwaltung)

PDF kein Volltext!
(Merkzettel, Notizen)

RIS Endnote, Citavi u.a.
(Literaturverwaltung)

MODS
(XML zur Weiterverarbeitung)

oder

Wählen Sie das für Sie passende Zitationsformat und kopieren Sie es dann in die Zwischenablage, lassen es sich per Mail zusenden oder speichern es als PDF-Datei.

Gewünschter Zitations-Stil:

oder

Bitte prüfen Sie, ob die Zitation formal korrekt ist, bevor Sie sie in einer Arbeit verwenden. Benutzen Sie gegebenenfalls den "Exportieren"-Dialog, wenn Sie ein Literaturverwaltungsprogramm verwenden und die Zitat-Angaben selbst formatieren wollen.

A quest for cytosolic sequons and their functions.