Repository logo
 

Hydrophobic-cationic peptides modulate RNA polymerase ribozyme activity by accretion.

Simple item page
cam.issuedOnline2022-06-03
dc.contributor.authorLi, Peiying
dc.contributor.authorHolliger, Philipp
dc.contributor.authorTagami, Shunsuke
dc.contributor.orcidLi, Peiying [0000-0002-0175-4600]
dc.contributor.orcidHolliger, Philipp [0000-0002-3440-9854]
dc.contributor.orcidTagami, Shunsuke [0000-0002-1720-3627]
dc.date.accessioned2022-06-07T08:13:00Z
dc.date.available2022-06-07T08:13:00Z
dc.date.issued2022-06-03
dc.date.submitted2021-03-07
dc.date.updated2022-06-07T08:12:58Z
dc.descriptionFunder: the Astrobiology Center of National Institutes of Natural Sciences (AB301005)
dc.description.abstractAccretion and the resulting increase in local concentration is a widespread mechanism in biology to enhance biomolecular functions (for example, in liquid-liquid demixing phases). Such macromolecular aggregation phases (e.g., coacervates, amyloids) may also have played a role in the origin of life. Here, we report that a hydrophobic-cationic RNA binding peptide selected by phage display (P43: AKKVWIIMGGS) forms insoluble amyloid-containing aggregates, which reversibly accrete RNA on their surfaces in an RNA-length and Mg2+-concentration dependent manner. The aggregates formed by P43 or its sequence-simplified version (K2V6: KKVVVVVV) inhibited RNA polymerase ribozyme (RPR) activity at 25 mM MgCl2, while enhancing it significantly at 400 mM MgCl2. Our work shows that such hydrophobic-cationic peptide aggregates can reversibly concentrate RNA and enhance the RPR activity, and suggests that they could have aided the emergence and evolution of longer and functional RNAs in the fluctuating environments of the prebiotic earth.
dc.identifier.doi10.17863/CAM.85194
dc.identifier.eissn2041-1723
dc.identifier.issn2041-1723
dc.identifier.others41467-022-30590-3
dc.identifier.other30590
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/337785
dc.languageen
dc.publisherSpringer Science and Business Media LLC
dc.subjectArticle
dc.subject/631/45/611
dc.subject/631/45/500
dc.subject/631/181/904
dc.subject/82/75
dc.subjectarticle
dc.titleHydrophobic-cationic peptides modulate RNA polymerase ribozyme activity by accretion.
dc.typeArticle
dcterms.dateAccepted2022-05-04
prism.issueIdentifier1
prism.publicationNameNat Commun
prism.volume13
pubs.funder-project-idMEXT | Japan Society for the Promotion of Science (JSPS) (20K14599, 18H01328)
pubs.funder-project-idRCUK | Medical Research Council (MRC) (MC_U105178804)
rioxxterms.licenseref.urihttp://creativecommons.org/licenses/by/4.0/
rioxxterms.versionVoR
rioxxterms.versionofrecord10.1038/s41467-022-30590-3

Files

Original bundle
Now showing 1 - 5 of 5
Thumbnail Image
Name:
41467_2022_30590_MOESM1_ESM.pdf
Size:
16.12 MB
Format:
Adobe Portable Document Format
Description:
Published version
Licence
http://creativecommons.org/licenses/by/4.0/
Download
Thumbnail Image
Name:
41467_2022_Article_30590.pdf
Size:
2.2 MB
Format:
Adobe Portable Document Format
Description:
Published version
Licence
http://creativecommons.org/licenses/by/4.0/
Download
No Thumbnail Available
Name:
additional-files.zip
Size:
80.37 MB
Format:
ZIP file
Description:
Supporting information
Licence
http://creativecommons.org/licenses/by/4.0/
Download
No Thumbnail Available
Name:
41467_2022_Article_30590_nlm.xml
Size:
116.72 KB
Format:
Extensible Markup Language
Description:
Bibliographic metadata
Licence
http://creativecommons.org/licenses/by/4.0/
Download
Thumbnail Image
Name:
41467_2022_30590_MOESM2_ESM.pdf
Size:
1.63 MB
Format:
Adobe Portable Document Format
Description:
Published version
Licence
http://creativecommons.org/licenses/by/4.0/
Download

Collections

Jisc Publications Router