Evidence map›Paper›PMID 24253588›Full record

ArticleNature communications2013

Analogue encoding of physicochemical properties of proteins in their cognate messenger RNAs.

Anton A Polyansky, Mario Hlevnjak, Bojan Zagrovic

Abstract read
In one paragraph

Article in Nature communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed.

  1. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Anton A PolyanskyDepartment of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria.
Mario Hlevnjak
Bojan Zagrovic

Funding

Austrian Science Fund FWF Y 514European Research Council 279408
6 · The paper itself

Abstract

Being related by the genetic code, mRNAs and their cognate proteins exhibit mutually interdependent compositions, which implies the possibility of a direct connection between their general physicochemical properties. Here we probe the general potential of the cell to encode information about proteins in the average characteristics of their cognate mRNAs and decode it in a ribosome-independent manner. We show that average protein hydrophobicity, calculated from either sequences or 3D structures, can be encoded in an analogue fashion by many different average mRNA sequence properties with the only constraint being that pyrimidine and purine bases be clearly distinguishable on average. Moreover, average characteristics of mRNA sequences enable discrimination between cytosolic and membrane proteins even in the absence of topogenic signal-based mechanisms. Our results suggest that protein and mRNA localization may be partly determined by basic physicochemical rationales and interdependencies between the two biomolecules.

Indexed as

Amino Acid SequenceGene Expression RegulationHydrophobic and Hydrophilic InteractionsModels, MolecularProtein ConformationProteinsRNA, MessengerProteinsRNA, Messenger

Identifiers

PMID24253588
PMCPMC3868254

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.