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Folding behavior of four silks of giant honey bee reflects the evolutionary conservation of aculeate silk proteins

Maitip, Jakkrawut; Trueman, Holly E.; Kaehler, Benjamin; Huttley, Gavin Austin; Chantawannakul, Panuwan; Sutherland, Tara D.

Description

Multiple gene duplication events in the precursor of the Aculeata (bees, ants, hornets) gave rise to four silk genes. Whilst these homologs encode proteins with similar amino acid composition and coiled coil structure, the retention of all four homologs implies they each are important. In this study we identified, produced and characterized the four silk proteins from Apis dorsata, the giant Asian honeybee. The proteins were readily purified, allowing us to investigate the folding behavior of...[Show more]

dc.contributor.authorMaitip, Jakkrawut
dc.contributor.authorTrueman, Holly E.
dc.contributor.authorKaehler, Benjamin
dc.contributor.authorHuttley, Gavin Austin
dc.contributor.authorChantawannakul, Panuwan
dc.contributor.authorSutherland, Tara D.
dc.date.accessioned2016-06-14T23:20:55Z
dc.identifier.issn0965-1748
dc.identifier.urihttp://hdl.handle.net/1885/103615
dc.description.abstractMultiple gene duplication events in the precursor of the Aculeata (bees, ants, hornets) gave rise to four silk genes. Whilst these homologs encode proteins with similar amino acid composition and coiled coil structure, the retention of all four homologs implies they each are important. In this study we identified, produced and characterized the four silk proteins from Apis dorsata, the giant Asian honeybee. The proteins were readily purified, allowing us to investigate the folding behavior of solutions of individual proteins in comparison to mixtures of all four proteins at concentrations where they assemble into their native coiled coil structure. In contrast to solutions of any one protein type, solutions of a mixture of the four proteins formed coiled coils that were stable against dilution and detergent denaturation. The results are consistent with the formation of a heteromeric coiled coil protein complex. The mechanism of silk protein coiled coil formation and evolution is discussed in light of these results.
dc.publisherPergamon-Elsevier Ltd
dc.sourceInsect Biochemistry and Molecular Biology
dc.titleFolding behavior of four silks of giant honey bee reflects the evolutionary conservation of aculeate silk proteins
dc.typeJournal article
local.description.notesImported from ARIES
local.identifier.citationvolume59
dc.date.issued2015
local.identifier.absfor060305 - Evolution of Developmental Systems
local.identifier.absfor060405 - Gene Expression (incl. Microarray and other genome-wide approaches)
local.identifier.ariespublicationU3488905xPUB8603
local.type.statusPublished Version
local.contributor.affiliationMaitip, Jakkrawut, Chiang Mai University
local.contributor.affiliationTrueman, Holly E., CSIRO Ecosystem Sciences
local.contributor.affiliationKaehler, Benjamin, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationHuttley, Gavin Austin, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationChantawannakul, Panuwan, Chiang Mai University
local.contributor.affiliationSutherland, Tara D., CSIRO
local.description.embargo2037-12-31
local.bibliographicCitation.startpage72
local.bibliographicCitation.lastpage79
local.identifier.doi10.1016/j.ibmb.2015.02.007
dc.date.updated2016-06-14T08:54:12Z
local.identifier.scopusID2-s2.0-84943162759
CollectionsANU Research Publications

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