Petunia nectar proteins have ribonuclease activity

dc.contributor.author Hillwig, Melissa
dc.contributor.author Liu, Xiaoteng
dc.contributor.author Macintosh, Gustavo
dc.contributor.author Liu, Guangyu
dc.contributor.author Thornburg, Robert
dc.contributor.author Macintosh, Gustavo
dc.contributor.department Biochemistry, Biophysics and Molecular Biology
dc.date 2018-02-17T11:07:56.000
dc.date.accessioned 2020-06-29T23:47:12Z
dc.date.available 2020-06-29T23:47:12Z
dc.date.copyright Fri Jan 01 00:00:00 UTC 2010
dc.date.issued 2010-01-01
dc.description.abstract <p>Plants requiring an insect pollinator often produce nectar as a reward for the pollinator's visitations. This rich secretion needs mechanisms to inhibit microbial growth. In <em>Nicotiana</em> spp. nectar, anti-microbial activity is due to the production of hydrogen peroxide. In a close relative, <em>Petunia hybrida</em>, limited production of hydrogen peroxide was found; yet petunia nectar still has anti-bacterial properties, suggesting that a different mechanism may exist for this inhibition. The nectar proteins of petunia plants were compared with those of ornamental tobacco and significant differences were found in protein profiles and function between these two closely related species. Among those proteins, RNase activities unique to petunia nectar were identified. The genes corresponding to four RNase T2 proteins from <em>Petunia hybrida</em> that show unique expression patterns in different plant tissues were cloned. Two of these enzymes, RNase Phy3 and RNase Phy4 are unique among the T2 family and contain characteristics similar to both S- and S-like RNases. Analysis of amino acid patterns suggest that these proteins are an intermediate between S- and S-like RNases, and support the hypothesis that S-RNases evolved from defence RNases expressed in floral parts. This is the first report of RNase activities in nectar.</p>
dc.description.comments <p>This is an article from <em>Journal of Experimental Botany</em> 61 (2010): 2951, doi:<a href="http://dx.doi.org/10.1093/jxb/erq119" target="_blank">10.1093/jxb/erq119</a>. Posted with permission.</p>
dc.format.mimetype application/pdf
dc.identifier archive/lib.dr.iastate.edu/bbmb_ag_pubs/48/
dc.identifier.articleid 1059
dc.identifier.contextkey 8045025
dc.identifier.s3bucket isulib-bepress-aws-west
dc.identifier.submissionpath bbmb_ag_pubs/48
dc.identifier.uri https://dr.lib.iastate.edu/handle/20.500.12876/10779
dc.language.iso en
dc.source.bitstream archive/lib.dr.iastate.edu/bbmb_ag_pubs/48/2010_MacIntosh_PetuniaNectar.pdf|||Sat Jan 15 00:27:05 UTC 2022
dc.source.uri 10.1093/jxb/erq119
dc.subject.disciplines Biochemistry, Biophysics, and Structural Biology
dc.subject.keywords Nectar
dc.subject.keywords nectarin
dc.subject.keywords nectary
dc.subject.keywords petunia
dc.subject.keywords ribonuclease
dc.subject.keywords RNase T2
dc.title Petunia nectar proteins have ribonuclease activity
dc.type article
dc.type.genre article
dspace.entity.type Publication
relation.isAuthorOfPublication 6879aca5-82d6-4301-ac56-17db07ad2bb8
relation.isOrgUnitOfPublication c70f85ae-e0cd-4dce-96b5-4388aac08b3f
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