NDLI: Dual location of a family of proteinase inhibitors within the stigmas of Nicotiana alata

Content Provider	Springer Nature Link
Author	Johnson, Elizabeth D. Miller, Elizabeth A. Anderson, Marilyn A.
Copyright Year	2006
Abstract	Reproductive and storage tissues of many plants produce large amounts of serine proteinase inhibitors (PIs). The ornamental tobacco, Nicotiana alata, produces a series of 6 kDa chymotrypsin and trypsin inhibitors that accumulate to up to 30% of soluble protein in the stigma. These inhibitors are derived by proteolytic processing of two closely related multidomain precursor proteins. Using immunogold electron microscopy, we find that the stigmatic PIs accumulate in both the central vacuole and in the extracellular mucilage. Labelling with antibodies specific for the C-terminal vacuolar targeting peptide (VTS) of each precursor confirms earlier biochemical data showing that the VTS is removed during passage through the secretory pathway. We have isolated and characterised the extracellular population of PIs, which are largely identical to PIs isolated from whole stigmas and are functional inhibitors of serine proteases. Subcellular fractionation of immature stigmas reveals that a sub-population of the PI precursor protein is proteolytically processed within the endoplasmic reticulum. This proteolysis results in the removal of the vacuolar sorting information, causing secretion of this PI population. We propose a novel mechanism whereby a single gene product may be simultaneously trafficked to two separate compartments mediated by proteolysis early in the secretory pathway.
Starting Page	1265
Ending Page	1276
Page Count	12
File Format	PDF
ISSN	00320935
Journal	Planta
Volume Number	225
Issue Number	5
e-ISSN	14322048
Language	English
Publisher	Springer-Verlag
Publisher Date	2006-10-20
Publisher Place	Berlin/Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Vacuole Endoplasmic reticulum Exudate Localization Proteinase inhibitors Stigma Forestry Ecology Agriculture Plant Sciences
Content Type	Text
Resource Type	Article
Subject	Genetics Plant Science

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Identification of a novel four-domain member of the proteinase inhibitor II family from the stigmas of Nicotiana alata

Independently silencing two JAR family members impairs levels of trypsin proteinase inhibitors but not nicotine

Evolution of proteinase inhibitor defenses in North American allopolyploid species of Nicotiana

Changes in electron transport pathways in endoplasmic reticulum of rapeseed in response to cold

Isolation and identification of cytoskeleton-associated prolamine mRNA binding proteins from developing rice seeds

Expression of OsBiP4 and OsBiP5 is highly correlated with the endoplasmic reticulum stress response in rice

Proteinase inhibitors in Nicotiana alata stigmas are derived from a precursor protein which is processed into five homologous inhibitors.

Expression and localization of calreticulin in tobacco anthers and pollen tubes

Processing and trafficking of a single isoform of the aspartic proteinase cardosin A on the vacuolar pathway

Dual location of a family of proteinase inhibitors within the stigmas of Nicotiana alata

Similar Documents

Identification of a novel four-domain member of the proteinase inhibitor II family from the stigmas of Nicotiana alata

Independently silencing two JAR family members impairs levels of trypsin proteinase inhibitors but not nicotine

Evolution of proteinase inhibitor defenses in North American allopolyploid species of Nicotiana

Changes in electron transport pathways in endoplasmic reticulum of rapeseed in response to cold

Isolation and identification of cytoskeleton-associated prolamine mRNA binding proteins from developing rice seeds

Expression of OsBiP4 and OsBiP5 is highly correlated with the endoplasmic reticulum stress response in rice

Proteinase inhibitors in Nicotiana alata stigmas are derived from a precursor protein which is processed into five homologous inhibitors.

Expression and localization of calreticulin in tobacco anthers and pollen tubes

Processing and trafficking of a single isoform of the aspartic proteinase cardosin A on the vacuolar pathway

Dual location of a family of proteinase inhibitors within the stigmas of Nicotiana alata