In Vitro Processing of Tomato Proteinase Inhibitor I by Barley Microsomal Membranes

Autor:	Liliane Sticher, Russell L. Jones, Alan B. Bennett, Katherine W. Osteryoung
Rok vydání:	1992
Předmět:	chemistry.chemical_classification Signal peptide Cellular and Structural Biology Physiology Sequence analysis food and beverages Plant Science Biology Cleavage (embryo) Membrane Enzyme Membrane protein chemistry Biochemistry Aleurone Genetics Endomembrane system
Zdroj:	Plant Physiology. 99:378-382
ISSN:	1532-2548 0032-0889
DOI:	10.1104/pp.99.2.378
Popis:	A plant-derived in vitro system for the study of cotranslational processing of plant endomembrane proteins has been developed and used to investigate cotranslational proteolytic processing of tomato proteinase inhibitor I. Translation of the inhibitor I precursor in wheat germ lysate supplemented with barley aleurone microsomal membranes resulted in cotranslational import of the protein into microsomal vesicles and cleavage of the signal sequence. NH(2)-terminal sequence analysis of the translocated inhibitor I processing intermediate showed that the signal sequence was cleaved between Ala(23) and Arg(24) of the precursor protein. Parallel experiments using dog pancreas microsomal membranes indicated an identical site of cleavage, suggesting that the substrate determinants for signal sequence processing are conserved across kingdoms. The plant-derived processing system used for this study may be valuable for analysis of cotranslational processing of other plant preproteins and for characterizing the components of the cotranslational import machinery in plants.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0f7117dae7c18f0fdf7226cecf66859 https://doi.org/10.1104/pp.99.2.378 Zobrazit plný text záznamu