MassIVE MSV000081716

Imported Reanalysis Dataset Public PXD002476

Arabidopsis chloroplast N-terminome

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Description

Protein N-termini are prone to post translational modification and are major determinants of protein stability in bacteria, eukaryotes, and perhaps also in chloroplasts. Most chloroplast proteins undergo N-terminal maturation, but this is poorly understood due to insufficient experimental information and the N-termini of mature chloroplast proteins cannot be accurately predicted. This motivated an extensive characterization of chloroplast protein N-termini using terminal amine isotopic labeling of substrates (TAILS). Many nuclear-encoded plastid proteins accumulated with two or three different N-termini; we evaluated the significance of these different proteoforms. Ala, Val, Thr (often in N-Î? acetylated form) and Ser were the most frequently observed N-terminal residues, even after normalization for their frequency in the plastid proteome, while other residues were absent or highly under-represented. Plastid-encoded proteins showed a similar distribution of N-terminal residues, but with a higher frequency of Met. Infrequent residues such as Ile, Arg, Cys, Pro, Asp and Glu were observed for several abundant proteins likely reflecting functional regulation through their N-termini. In contrast, the thylakoid lumenal proteome showed a wide diversity of N-terminal residues, including those typically associated with instability (Asp, Glu, Leu, Phe). We propose that after cleavage of the chloroplast transit peptide by stromal processing peptidase, additional processing by unidentified peptidases occurs to avoid unstable or otherwise unfavorable N-terminal residues. The possibility of a chloroplast N-end rule is discussed. This work provides a baseline for understanding N-terminal processing and maturation of chloroplast proteins. [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: N-terminome ; Arabidopsis thaliana ; proteolysis ; protein maturation ; protein processing ; chloroplast protein import ; chloroplast transit peptide ; TAILS

Contact

Principal Investigators:
(in alphabetical order) 		Klaas van Wijk, Dept. Plant Biology Cornell University, N/A
Submitting User: ccms

Publications

Rowland E, Kim J, Bhuiyan NH, van Wijk KJ.
The Arabidopsis Chloroplast Stromal N-Terminome: Complexities of Amino-Terminal Protein Maturation and Stability.
Plant Physiol. 2015 Nov;169(3):1881-96. Epub 2015 Sep 14.

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