Dataset Information

An atypical aspartic protease modulates lateral root development in Arabidopsis thaliana

ABSTRACT: We determined the specificity profile of recombinant ASPR1 (Atypical Aspartic Protease in Roots 1) using proteome-derived libraries. Although rASPR1 preferred hydrophobic amino acids in the S1 subsite, which is in line with what was previously described for other APs, rASPR1 also displayed a clear preference for accommodating asparagine and lysine in S1, a characteristic only reported so far for fungal APs. Both primary and secondary specificity preferences of rASPR1 thus revealed unique specificity requirements similar to fungal APs that are unprecedented for plant APs.

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Suspension Culture, Blood Cell, Monocyte, Blood

SUBMITTER: Sandra Anjo

LAB HEAD: Isaura Simões

PROVIDER: PXD010355 | Pride | 2020-03-19

REPOSITORIES: pride

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			Action	DRS
	20140110_84GluC_10uL_CXPColumn_SET13.tandem.interact.ipro.pep.xls	Xls
	5_GluC_10uL_SET13.mzXML	Mzxml
	5_GluC_10uL_SET13.wiff	Wiff
	5_GluC_10uL_SET13.wiff.scan	Wiff
	5_Tryp_10uL_SET14.mzXML	Mzxml

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An atypical aspartic protease modulates lateral root development in Arabidopsis thaliana.

Soares André A Niedermaier Stefan S Faro Rosário R Loos Andreas A Manadas Bruno B Faro Carlos C Huesgen Pitter F PF Cheung Alice Y AY Simões Isaura I

Journal of experimental botany 20190401 7

Few atypical aspartic proteases (APs) present in plants have been functionally studied to date despite having been implicated in developmental processes and stress responses. Here we characterize a novel atypical AP that we name Atypical Aspartic Protease in Roots 1 (ASPR1), denoting its expression in Arabidopsis roots. Recombinant ASPR1 produced by transient expression in Nicotiana benthamiana was active and displayed atypical properties, combining optimum acidic pH, partial sensitivity to peps ...[more]

PMID: 30778561

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