Deletion of the N-terminal dirigent domain in maize beta-glucosidase aggregating factor and its homolog sorghum lectin dramatically alters the sugar-specificities of their lectin domains

Copyright 2010 Elsevier Masson SAS. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Plant physiology and biochemistry : PPB. - 1991. - 48(2010), 8 vom: 01. Aug., Seite 731-4
1. Verfasser: Kittur, Farooqahmed S (VerfasserIn)
Weitere Verfasser: Yu, Hyun Young, Bevan, David R, Esen, Asim
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2010
Zugriff auf das übergeordnete Werk:Plant physiology and biochemistry : PPB
Schlagworte:Journal Article Research Support, U.S. Gov't, Non-P.H.S. BGAF protein, Zea mays Carrier Proteins Lectins Plant Proteins Fructose 30237-26-4 Glucose IY9XDZ35W2 mehr... Lactose J2B2A4N98G Acetylgalactosamine KM15WK8O5T Mannose PHA4727WTP Galactose X2RN3Q8DNE
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100 1 |a Kittur, Farooqahmed S  |e verfasserin  |4 aut 
245 1 0 |a Deletion of the N-terminal dirigent domain in maize beta-glucosidase aggregating factor and its homolog sorghum lectin dramatically alters the sugar-specificities of their lectin domains 
264 1 |c 2010 
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500 |a Date Revised 30.09.2020 
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520 |a Copyright 2010 Elsevier Masson SAS. All rights reserved. 
520 |a Maize beta-glucosidase aggregating factor (BGAF) and its homolog Sorghum Lectin (SL) are modular proteins consisting of an N-terminal dirigent domain and a C-terminal jacalin-related lectin (JRL) domain. BGAF is a polyspecific lectin with a monosaccharide preference for galactose, whereas SL displays preference for GalNAc. Here, we report that deletion of the N-terminal dirigent domain in the above lectins dramatically changes their sugar-specificities. Deletions in the N-terminal region of the dirigent domain of BGAF abolished binding to galactose/lactose, but binding to mannose was unaffected. Glucose, which was a poor inhibitor of hemagglutinating activity of BGAF, displayed higher inhibitory effect on the hemagglutinating activity of deletion mutants. Deletion of the dirigent domain in SL abolished binding to GalNAc, but binding to mannose was not affected. Surprisingly, fructose, an extremely poor inhibitor (minimum inhibitory concentration (MIC) = 125 mM) of SL hemagglutinating activity, was found to be a very potent inhibitor (MIC = 1 mM) of hemagglutinating activity of its JRL domain. These results indicate that the dirigent domain in this class of modular lectins, at least in the case of maize BGAF and SL, influences sugar specificity 
650 4 |a Journal Article 
650 4 |a Research Support, U.S. Gov't, Non-P.H.S. 
650 7 |a BGAF protein, Zea mays  |2 NLM 
650 7 |a Carrier Proteins  |2 NLM 
650 7 |a Lectins  |2 NLM 
650 7 |a Plant Proteins  |2 NLM 
650 7 |a Fructose  |2 NLM 
650 7 |a 30237-26-4  |2 NLM 
650 7 |a Glucose  |2 NLM 
650 7 |a IY9XDZ35W2  |2 NLM 
650 7 |a Lactose  |2 NLM 
650 7 |a J2B2A4N98G  |2 NLM 
650 7 |a Acetylgalactosamine  |2 NLM 
650 7 |a KM15WK8O5T  |2 NLM 
650 7 |a Mannose  |2 NLM 
650 7 |a PHA4727WTP  |2 NLM 
650 7 |a Galactose  |2 NLM 
650 7 |a X2RN3Q8DNE  |2 NLM 
700 1 |a Yu, Hyun Young  |e verfasserin  |4 aut 
700 1 |a Bevan, David R  |e verfasserin  |4 aut 
700 1 |a Esen, Asim  |e verfasserin  |4 aut 
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773 1 8 |g volume:48  |g year:2010  |g number:8  |g day:01  |g month:08  |g pages:731-4 
856 4 0 |u http://dx.doi.org/10.1016/j.plaphy.2010.03.007  |3 Volltext 
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