Barley cysteine protease PAP14 plays a role in degradation of chloroplast proteins.
Chloroplast Proteins
/ metabolism
Chloroplasts
/ metabolism
Cysteine Proteases
/ metabolism
Endoplasmic Reticulum
/ metabolism
Hordeum
/ enzymology
Hydrogen-Ion Concentration
Models, Biological
Plant Leaves
/ metabolism
Plants, Genetically Modified
Protein Transport
Proteolysis
Recombinant Proteins
/ metabolism
Substrate Specificity
Hordeum vulgare L
Barley
HvPAP14 (CAQ00109.1)
Rubisco
chloroplast
cysteine protease
leaf senescence
thylakoid membranes
Journal
Journal of experimental botany
ISSN: 1460-2431
Titre abrégé: J Exp Bot
Pays: England
ID NLM: 9882906
Informations de publication
Date de publication:
18 11 2019
18 11 2019
Historique:
received:
04
06
2019
accepted:
31
07
2019
pubmed:
14
8
2019
medline:
11
8
2020
entrez:
13
8
2019
Statut:
ppublish
Résumé
Chloroplast protein degradation is known to occur both inside chloroplasts and in the vacuole. Genes encoding cysteine proteases have been found to be highly expressed during leaf senescence. However, it remains unclear where they participate in chloroplast protein degradation. In this study HvPAP14, which belongs to the C1A family of cysteine proteases, was identified in senescing barley (Hordeum vulgare L.) leaves by affinity enrichment using the mechanism-based probe DCG-04 targeting cysteine proteases and subsequent mass spectrometry. Biochemical analyses and expression of a HvPAP14:RFP fusion construct in barley protoplasts was used to identify the subcellular localization and putative substrates of HvPAP14. The HvPAP14:RFP fusion protein was detected in the endoplasmic reticulum and in vesicular bodies. Immunological studies showed that HvPAP14 was mainly located in chloroplasts, where it was found in tight association with thylakoid membranes. The recombinant enzyme was activated by low pH, in accordance with the detection of HvPAP14 in the thylakoid lumen. Overexpression of HvPAP14 in barley revealed that the protease can cleave LHCB proteins and PSBO as well as the large subunit of Rubisco. HvPAP14 is involved in the normal turnover of chloroplast proteins and may have a function in bulk protein degradation during leaf senescence.
Identifiants
pubmed: 31403664
pii: 5546963
doi: 10.1093/jxb/erz356
pmc: PMC6859807
doi:
Substances chimiques
Chloroplast Proteins
0
Recombinant Proteins
0
Cysteine Proteases
EC 3.4.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
6057-6069Informations de copyright
© The Author(s) 2019. Published by Oxford University Press on behalf of the Society for Experimental Biology.
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