Evidence map›Paper›PMID 26152732›Full record

ArticleJournal of biochemistry2016

Functional implication of archaeal homologues of human RNase P protein pair Pop5 and Rpp30.

Masato Hamasaki, Kohsuke Hazeyama, Fumihiko Iwasaki, Toshifumi Ueda, Takashi Nakashima, Yoshimitsu Kakuta, Makoto Kimura

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.8field-weighted citation impact, top 27% of its field
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

2 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Review
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

7 authors at 1 institution in 1 country.

Masato HamasakiLaboratory of Biochemistry, Department of Bioscience and Biotechnology, Graduate School, Faculty of Agriculture, Kyushu University, 6-10-1 Hakozaki, Fukuoka 812-8581, Japan and.
Kohsuke HazeyamaLaboratory of Biochemistry, Department of Bioscience and Biotechnology, Graduate School, Faculty of Agriculture, Kyushu University, 6-10-1 Hakozaki, Fukuoka 812-8581, Japan and.
Fumihiko IwasakiLaboratory of Structural Biology, Division of Bioengineering, Graduate School of Systems Life Sciences, 6-10-1 Hakozaki, Fukuoka 812-8581, Japan.
Toshifumi UedaLaboratory of Structural Biology, Division of Bioengineering, Graduate School of Systems Life Sciences, 6-10-1 Hakozaki, Fukuoka 812-8581, Japan.
Takashi NakashimaLaboratory of Biochemistry, Department of Bioscience and Biotechnology, Graduate School, Faculty of Agriculture, Kyushu University, 6-10-1 Hakozaki, Fukuoka 812-8581, Japan and Laboratory of Structural Biology, Division of Bioengineering, Graduate School of Systems Life Sciences, 6-10-1 Hakozaki, Fukuoka 812-8581, Japan.
Yoshimitsu KakutaLaboratory of Biochemistry, Department of Bioscience and Biotechnology, Graduate School, Faculty of Agriculture, Kyushu University, 6-10-1 Hakozaki, Fukuoka 812-8581, Japan and Laboratory of Structural Biology, Division of Bioengineering, Graduate School of Systems Life Sciences, 6-10-1 Hakozaki, Fukuoka 812-8581, Japan.
Makoto KimuraLaboratory of Biochemistry, Department of Bioscience and Biotechnology, Graduate School, Faculty of Agriculture, Kyushu University, 6-10-1 Hakozaki, Fukuoka 812-8581, Japan and Laboratory of Structural Biology, Division of Bioengineering, Graduate School of Systems Life Sciences, 6-10-1 Hakozaki, Fukuoka 812-8581, Japan mkimura@agr.kyushu-u.ac.jp.
Kyushu University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PhoPop5 and PhoRpp30 in the hyperthermophilic archaeon Pyrococcus horikoshii, homologues of human ribonuclease P (RNase P) proteins hPop5 and Rpp30, respectively, fold into a heterotetramer [PhoRpp30-(PhoPop5)2-PhoRpp30], which plays a crucial role in the activation of RNase P RNA (PhopRNA). Here, we examined the functional implication of PhoPop5 and PhoRpp30 in the tetramer. Surface plasmon resonance (SPR) analysis revealed that the tetramer strongly interacts with an oligonucleotide including the nucleotide sequence of a stem-loop SL3 in PhopRNA. In contrast, PhoPop5 had markedly reduced affinity to SL3, whereas PhoRpp30 had little affinity to SL3. SPR studies of PhoPop5 mutants further revealed that the C-terminal helix (α4) in PhoPop5 functions as a molecular recognition element for SL3. Moreover, gel filtration indicated that PhoRpp30 exists as a monomer, whereas PhoPop5 is an oligomer in solution, suggesting that PhoRpp30 assists PhoPop5 in attaining a functionally active conformation by shielding hydrophobic surfaces of PhoPop5. These results, together with available data, allow us to generate a structural and mechanistic model for the PhopRNA activation by PhoPop5 and PhoRpp30, in which the two C-terminal helices (α4) of PhoPop5 in the tetramer whose formation is assisted by PhoRpp30 act as binding elements and bridge SL3 and SL16 in PhopRNA.

Indexed as

Protein Structure, TertiaryArchaeal ProteinsAutoantigensBase SequenceHumansKineticsMolecular ChaperonesProtein SubunitsPyrococcus horikoshiiRibonuclease PRNA, ArchaealSurface Plasmon ResonanceArchaeal ProteinsAutoantigensMolecular ChaperonesPop5 protein, humanProtein SubunitsRibonuclease PRNA, ArchaealRPP30 protein, humanarchaeaprotein–RNA interactionPyrococcus horikoshiiribonuclease Psurface plasmon resonance

Identifiers

PMID26152732
PMCPMC4882637
OpenAlexW2312807137

What OpenQuestion holds

Textmetadata
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.