NDLI: A rice lipid transfer protein binds to plasma membrane proteinaceous sites

Content Provider	Springer Nature Link
Author	Wang, Xiaofeng Wang, Hai Li, Yuanli Cao, Kaiming Ge, Xiaochun
Copyright Year	2008
Abstract	Nonspecific lipid transfer protein (nsLTP) is usually basic and secreted low-molecular-mass protein in plants. The 3-D structure of nsLTP1 resembles that of elicitin produced by the plant pathogen Phytophthora cryptogea, which can bind to the plant plasma membrane putative receptor and activate the downstream responses. It is inferred that nsLTP1 may have similar binding sites on the plasma membranes. In this work, rice recombinant protein TRX-nsLTP110 labeled with $^{125}$I was shown to bind to rice plasma membrane preparations in a saturable curve, with an apparent K$_{d}$ of 13.6 nM and B$_{max}$ of 150 fmol/mg proteins. Competition experiments revealed that the binding of TRX-nsLTP110 was specific, in contrast to the nonspecific binding of the fusion tag thioredoxin. Protease treatment assay showed that the binding sites were proteinaceous. Our results suggest that the binding sites of nsLTPs on plasma membranes may be ubiquitous in the plant kingdom. They may be competed out from the binding sites under pathogen attack, supporting a role for nsLTP1 in host defense response to pathogens.
Starting Page	745
Ending Page	750
Page Count	6
File Format	PDF
ISSN	03014851
Journal	Molecular Biology Reports
Volume Number	36
Issue Number	4
e-ISSN	15734978
Language	English
Publisher	Springer Netherlands
Publisher Date	2008-05-07
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Binding Nonspecific lipid transfer protein Plasma membrane preparations Receptor Rice Animal Biochemistry Animal Anatomy / Morphology / Histology
Content Type	Text
Resource Type	Article
Subject	Genetics Medicine Molecular Biology

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

RNA-binding protein Rbm47 binds to Nanog in mouse embryonic stem cells

Sulfadiazine binds and unfolds bovine serum albumin: an in vitro study

Molecular characterization of rice OsBIANK1, encoding a plasma membrane-anchored ankyrin repeat protein, and its inducible expression in defense responses

SBP, SECIS binding protein, binds to the RNA fragment upstream of the Sec UGA codon in glutathione peroxidase mRNA

Identification of functional PDZ domain binding sites in several human proteins

Effects of Acylation on the Structure, Lipid Binding, and Transfer Activity of Wheat Lipid Transfer Protein

A potato pathogenesis-related protein gene, StPRp27, contributes to race-nonspecific resistance against Phytophthora infestans

Lipid binding in rice nonspecific lipid transfer protein-1 complexes from Oryza sativa

Overproduction of mouse estrogen receptor alpha-ligand binding domain decreases bacterial growth

A rice lipid transfer protein binds to plasma membrane proteinaceous sites

Similar Documents

RNA-binding protein Rbm47 binds to Nanog in mouse embryonic stem cells

Sulfadiazine binds and unfolds bovine serum albumin: an in vitro study

Molecular characterization of rice OsBIANK1, encoding a plasma membrane-anchored ankyrin repeat protein, and its inducible expression in defense responses

SBP, SECIS binding protein, binds to the RNA fragment upstream of the Sec UGA codon in glutathione peroxidase mRNA

Identification of functional PDZ domain binding sites in several human proteins

Effects of Acylation on the Structure, Lipid Binding, and Transfer Activity of Wheat Lipid Transfer Protein

A potato pathogenesis-related protein gene, StPRp27, contributes to race-nonspecific resistance against Phytophthora infestans

Lipid binding in rice nonspecific lipid transfer protein-1 complexes from Oryza sativa

Overproduction of mouse estrogen receptor alpha-ligand binding domain decreases bacterial growth

A rice lipid transfer protein binds to plasma membrane proteinaceous sites