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Article: Identification of the binding and inhibition sites in the calmodulin molecule for ophiobolin A by site-directed mutagenesis

TitleIdentification of the binding and inhibition sites in the calmodulin molecule for ophiobolin A by site-directed mutagenesis
Authors
Issue Date1998
PublisherAmerican Society of Plant Biologists. The Journal's web site is located at http://www.plantphysiol.org
Citation
Plant Physiology, 1998, v. 118 n. 3, p. 965-973 How to Cite?
AbstractOphiobolin A, a fungal toxin that affects maize and rice, has previously been shown to inhibit calmodulin by reacting with the lysine (Lys) residues in the calmodulin. In the present study we mutated Lys-75, Lys-77, and Lys-148 in the calmodulin molecule by site-directed mutagenesis, either by deleting them or by changing them to glutamine or arginine. We found that each of these three Lys residues could bind one molecule of ophiobolin A. Normally, only Lys-75 and Lys-148 bind ophiobolin A. Lys-77 seemed to be blocked by the binding of ophiobolin A to Lys-75. Lys-75 is the primary binding site and is responsible for all of the inhibition of ophiobolin A. When Lys-75 was removed, Lys-77 could then react with ophiobolin A to produce inhibition. Lys-148 was shown to be a binding site but not an inhibition site. The Lys-75 mutants were partially resistant to ophiobolin A. When both Lys 75 and Lys-77 or all three Lys residues were mutated, the resulting calmodulins were very resistant to ophiobolin A. Furthermore, Lys residues added in positions 86 and/or 143 (which are highly conserved in plant calmodulins) did not react with ophiobolin A. None of the mutations seemed to affect the properties of calmodulin. These results show that ophiobolin A reacts quite specifically with calmodulin.
Persistent Identifierhttp://hdl.handle.net/10722/49359
ISSN
2015 Impact Factor: 6.28
2015 SCImago Journal Rankings: 3.642
PubMed Central ID

 

DC FieldValueLanguage
dc.contributor.authorAu, TKen_HK
dc.contributor.authorLeung, PCen_HK
dc.date.accessioned2008-06-12T06:40:18Z-
dc.date.available2008-06-12T06:40:18Z-
dc.date.issued1998en_HK
dc.identifier.citationPlant Physiology, 1998, v. 118 n. 3, p. 965-973en_HK
dc.identifier.issn0032-0889en_HK
dc.identifier.urihttp://hdl.handle.net/10722/49359-
dc.description.abstractOphiobolin A, a fungal toxin that affects maize and rice, has previously been shown to inhibit calmodulin by reacting with the lysine (Lys) residues in the calmodulin. In the present study we mutated Lys-75, Lys-77, and Lys-148 in the calmodulin molecule by site-directed mutagenesis, either by deleting them or by changing them to glutamine or arginine. We found that each of these three Lys residues could bind one molecule of ophiobolin A. Normally, only Lys-75 and Lys-148 bind ophiobolin A. Lys-77 seemed to be blocked by the binding of ophiobolin A to Lys-75. Lys-75 is the primary binding site and is responsible for all of the inhibition of ophiobolin A. When Lys-75 was removed, Lys-77 could then react with ophiobolin A to produce inhibition. Lys-148 was shown to be a binding site but not an inhibition site. The Lys-75 mutants were partially resistant to ophiobolin A. When both Lys 75 and Lys-77 or all three Lys residues were mutated, the resulting calmodulins were very resistant to ophiobolin A. Furthermore, Lys residues added in positions 86 and/or 143 (which are highly conserved in plant calmodulins) did not react with ophiobolin A. None of the mutations seemed to affect the properties of calmodulin. These results show that ophiobolin A reacts quite specifically with calmodulin.en_HK
dc.format.extent418 bytes-
dc.format.mimetypetext/html-
dc.languageengen_HK
dc.publisherAmerican Society of Plant Biologists. The Journal's web site is located at http://www.plantphysiol.orgen_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.subject.meshCalmodulin - chemistry - genetics - metabolismen_HK
dc.subject.meshTerpenes - metabolismen_HK
dc.subject.meshAmino Acid Substitutionen_HK
dc.subject.meshBase Sequenceen_HK
dc.subject.meshBinding Sitesen_HK
dc.titleIdentification of the binding and inhibition sites in the calmodulin molecule for ophiobolin A by site-directed mutagenesisen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0032-0889&volume=118&issue=3&spage=965&epage=973&date=1998&atitle=Identification+of+the+binding+and+inhibition+sites+in+the+calmodulin+molecule+for+ophiobolin+A+by+site-directed+mutagenesisen_HK
dc.identifier.emailLeung, PC: pcleung@hkucc.hku.hken_HK
dc.description.naturepublished_or_final_versionen_HK
dc.identifier.pmid9808741en_HK
dc.identifier.pmcidPMC34807-
dc.identifier.scopuseid_2-s2.0-0032199530-
dc.identifier.hkuros40395-

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