File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Site-directed mutagenesis shows the significance of interactions with phospholipids and the G-protein OsYchF1 for the physiological functions of the rice GTPase-Activating Protein 1 (OsGAP1)

TitleSite-directed mutagenesis shows the significance of interactions with phospholipids and the G-protein OsYchF1 for the physiological functions of the rice GTPase-Activating Protein 1 (OsGAP1)
Authors
KeywordsCrystal structure
G protein
Phospholipid
Plant defense
Plasma membrane
Issue Date2015
Citation
Journal of Biological Chemistry, 2015, v. 290 n. 39, p. 23984-23996 How to Cite?
AbstractThe C2 domain is one of the most diverse phospholipid-binding domains mediating cellular signaling. One group of C2-domain proteins are plant-specific and are characterized by their small sizes and simple structures. We have previously reported that a member of this group, OsGAP1, is able to alleviate salt stress and stimulate defense responses, and bind to both phospholipids and an unconventional G-protein, OsYchF1. Here we solved the crystal structure of OsGAP1 to a resolution of 1.63 Å. Using site-directed mutagenesis, we successfully differentiated between the clusters of surface residues that are required for binding to phospholipids versus OsYchF1, which, in turn, is critical for its role in stimulating defense responses. On the other hand, the ability to alleviate salt stress by OsGAP1 is dependent only on its ability to bind OsYchF1 and is independent of its phospholipid-binding activity.
Persistent Identifierhttp://hdl.handle.net/10722/222506
ISSN
2019 Impact Factor: 4.238
2015 SCImago Journal Rankings: 3.151
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorYung, YL-
dc.contributor.authorCheung, MY-
dc.contributor.authorMiao, R-
dc.contributor.authorFong, YH-
dc.contributor.authorLI, KP-
dc.contributor.authorYU, MH-
dc.contributor.authorChye, ML-
dc.contributor.authorWong, KB-
dc.contributor.authorLAM, HM-
dc.date.accessioned2016-01-18T07:41:48Z-
dc.date.available2016-01-18T07:41:48Z-
dc.date.issued2015-
dc.identifier.citationJournal of Biological Chemistry, 2015, v. 290 n. 39, p. 23984-23996-
dc.identifier.issn0021-9258-
dc.identifier.urihttp://hdl.handle.net/10722/222506-
dc.description.abstractThe C2 domain is one of the most diverse phospholipid-binding domains mediating cellular signaling. One group of C2-domain proteins are plant-specific and are characterized by their small sizes and simple structures. We have previously reported that a member of this group, OsGAP1, is able to alleviate salt stress and stimulate defense responses, and bind to both phospholipids and an unconventional G-protein, OsYchF1. Here we solved the crystal structure of OsGAP1 to a resolution of 1.63 Å. Using site-directed mutagenesis, we successfully differentiated between the clusters of surface residues that are required for binding to phospholipids versus OsYchF1, which, in turn, is critical for its role in stimulating defense responses. On the other hand, the ability to alleviate salt stress by OsGAP1 is dependent only on its ability to bind OsYchF1 and is independent of its phospholipid-binding activity.-
dc.languageeng-
dc.relation.ispartofJournal of Biological Chemistry-
dc.subjectCrystal structure-
dc.subjectG protein-
dc.subjectPhospholipid-
dc.subjectPlant defense-
dc.subjectPlasma membrane-
dc.titleSite-directed mutagenesis shows the significance of interactions with phospholipids and the G-protein OsYchF1 for the physiological functions of the rice GTPase-Activating Protein 1 (OsGAP1)-
dc.typeArticle-
dc.identifier.emailMiao, R: miaorui@hku.hk-
dc.identifier.emailChye, ML: mlchye@hkucc.hku.hk-
dc.identifier.authorityChye, ML=rp00687-
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1074/jbc.M115.655639-
dc.identifier.pmid26286751-
dc.identifier.pmcidPMC4583037-
dc.identifier.hkuros256704-
dc.identifier.volume290-
dc.identifier.issue39-
dc.identifier.spage23984-
dc.identifier.epage23996-
dc.identifier.isiWOS:000361816500042-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats