Linked Life Data

19371749

Source:http://linkedlifedata.com/resource/pubmed/id/19371749

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2009-5-29
pubmed:databankReference
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/AM403100, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/AM403101, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/FM876234, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/FM876235, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/FM876236, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/FM876237, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/FM876238, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/FM876239, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/FM876240, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X94987, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X94988, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X94989, http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X94990
pubmed:abstractText
In many insect species, odorant-binding proteins (OBPs) are thought to be responsible for the transport of pheromones and other semiochemicals across the sensillum lymph to the olfactory receptors (ORs) within the antennal sensilla. In the silkworm Bombyx mori, the OBPs are subdivided into three main subfamilies; pheromone-binding proteins (PBPs), general odorant-binding proteins (GOBPs) and antennal-binding proteins (ABPs). We used the MotifSearch algorithm to search for genes encoding putative OBPs in B. mori and found 13, many fewer than are found in the genomes of fruit flies and mosquitoes. The 13 genes include seven new ABP-like OBPs as well as the previously identified PBPs (three), GOBPs (two) and ABPx. Quantitative examination of transcript levels showed that BmorPBP1, BmorGOBP1, BmorGOBP2 and BmorABPx are expressed at very high levels in the antennae and so could be involved in olfaction. A new two-phase binding assay, along with other established assays, showed that BmorPBP1, BmorPBP2, BmorGOBP2 and BmorABPx all bind to the B. mori sex pheromone component (10E,12Z)-hexadecadien-1-ol (bombykol). BmorPBP1, BmorPBP2 and BmorABPx also bind the pheromone component (10E,12Z)-hexadecadienal (bombykal) equally well, whereas BmorGOBP2 can discriminate between bombykol and bombykal. X-ray structures show that when bombykol is bound to BmorGOBP2 it adopts a different conformation from that found when it binds to BmorPBP1. Binding to BmorGOBP2 involves hydrogen bonding to Arg110 rather than to Ser56 as found for BmorPBP1.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1089-8638
pubmed:author
pubmed:issnType
Electronic
pubmed:day
12
pubmed:volume
389
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
529-45
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Characterisation of Bombyx mori Odorant-binding proteins reveals that a general odorant-binding protein discriminates between sex pheromone components.
pubmed:affiliation
Department of Biological Chemistry, Rothamsted Research, Harpenden, AL5 2JQ, UK. jing-jiang.zhou@bbsrc.ac.uk
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't