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Searching N-terminal modifications of proteins starting with Gly in Arabidopsis thaliana

ABSTRACT: Characterization of Myristoylated proteins in Arabidopsis thaliana Col 0 wild type

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Plant Cell, Rosette

SUBMITTER: Willy Bienvenut

LAB HEAD: Willy Bienvenut

PROVIDER: PXD008663 | Pride | 2018-06-18

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	20130111_WIB_At-WT-Rep1_SCX_Frac-02.dat	Other
	20130111_WIB_At-WT-Rep1_SCX_Frac-02.mgf	Mgf
	20130111_WIB_At-WT-Rep1_SCX_Frac-02.raw	Raw
	20130111_WIB_At-WT-Rep1_SCX_Frac-03.dat	Other
	20130111_WIB_At-WT-Rep1_SCX_Frac-03.mgf	Mgf

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Publications

Structural and genomic decoding of human and plant myristoylomes reveals a definitive recognition pattern.

Castrec Benoit B Dian Cyril C Ciccone Sarah S Ebert Coralie L CL Bienvenut Willy V WV Le Caer Jean-Pierre JP Steyaert Jean-Marc JM Giglione Carmela C Meinnel Thierry T

Nature chemical biology 20180611 7

An organism's entire protein modification repertoire has yet to be comprehensively mapped. N-myristoylation (MYR) is a crucial eukaryotic N-terminal protein modification. Here we mapped complete Homo sapiens and Arabidopsis thaliana myristoylomes. The crystal structures of human modifier NMT1 complexed with reactive and nonreactive target-mimicking peptide ligands revealed unexpected binding clefts and a modifier recognition pattern. This information allowed integrated mapping of myristoylomes u ...[more]

PMID: 29892081

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