Evidence map›Paper›PMID 26265777›Full record

ArticlePlant physiology2015

Genetic and Physical Interaction Studies Reveal Functional Similarities between ALBINO3 and ALBINO4 in Arabidopsis.

Raphael Trösch, Mats Töpel, Úrsula Flores-Pérez, Paul Jarvis

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

17 citing papers in PubMed, 25 citations in OpenAlex.

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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

4 authors at 2 institutions in 1 country.

Raphael TröschDepartment of Biology, University of Leicester, Leicester LE1 7RH, United Kingdom (R.T., M.T., P.J.); andDepartment of Plant Sciences, University of Oxford, Oxford OX1 3RB, United Kingdom (U.F.-P., P.J.).
Mats TöpelDepartment of Biology, University of Leicester, Leicester LE1 7RH, United Kingdom (R.T., M.T., P.J.); andDepartment of Plant Sciences, University of Oxford, Oxford OX1 3RB, United Kingdom (U.F.-P., P.J.).
Úrsula Flores-PérezDepartment of Biology, University of Leicester, Leicester LE1 7RH, United Kingdom (R.T., M.T., P.J.); andDepartment of Plant Sciences, University of Oxford, Oxford OX1 3RB, United Kingdom (U.F.-P., P.J.).
Paul JarvisDepartment of Biology, University of Leicester, Leicester LE1 7RH, United Kingdom (R.T., M.T., P.J.); andDepartment of Plant Sciences, University of Oxford, Oxford OX1 3RB, United Kingdom (U.F.-P., P.J.) paul.jarvis@plants.ox.ac.uk.
University of Leicester · GBUniversity of Oxford · GB

Funding

Biotechnology and Biological Sciences Research Council BB/D016541/1Biotechnology and Biological Sciences Research Council BB/F020325/1Biotechnology and Biological Sciences Research Council BB/H008039/1
6 · The paper itself

Abstract

ALBINO3 (ALB3) is a well-known component of a thylakoid protein-targeting complex that interacts with the chloroplast signal recognition particle (cpSRP) and the cpSRP receptor, chloroplast filamentous temperature-sensitive Y (cpFtsY). Its protein-inserting function has been established mainly for light-harvesting complex proteins, which first interact with the unique chloroplast cpSRP43 component and then are delivered to the ALB3 integrase by a GTP-dependent cpSRP-cpFtsY interaction. In Arabidopsis (Arabidopsis thaliana), a subsequently discovered ALB3 homolog, ALB4, has been proposed to be involved not in light-harvesting complex protein targeting, but instead in the stabilization of the ATP synthase complex. Here, however, we show that ALB3 and ALB4 share significant functional overlap, and that both proteins are required for the efficient insertion of cytochrome f and potentially other subunits of pigment-bearing protein complexes. Genetic and physical interactions between ALB4 and ALB3, and physical interactions between ALB4 and cpSRP, suggest that the two ALB proteins may engage similar sets of interactors for their specific functions. We propose that ALB4 optimizes the insertion of thylakoid proteins by participating in the ALB3-cpSRP pathway for certain substrates (e.g. cytochrome f and the Rieske protein). Although ALB4 has clearly diverged from ALB3 in relation to the partner-recruiting C-terminal domain, our analysis suggests that one putative cpSRP-binding motif has not been entirely lost.

Indexed as

Amino Acid MotifsAmino Acid SequenceArabidopsisArabidopsis ProteinsChloroplastsCytochrome b6f ComplexMolecular Sequence DataMutationPhylogenyPlants, Genetically ModifiedSignal Recognition ParticleThylakoidsAlb4 protein, ArabidopsisALBINO 3 protein, ArabidopsisArabidopsis ProteinsCytochrome b6f ComplexSignal Recognition Particle

Identifiers

PMID26265777
PMCPMC4587442
OpenAlexW2142052586

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.