Characterization of a nucleic acid‐binding translin‐like protein localized to the basal body in the unicellular green alga <i>Chlamydomonas reinhardtii</i>

This study characterizes a translin-like protein from Chlamydomonas reinhardtii, a unicellular alga. The efficient binding of the Crtranslin protein to both single-stranded DNA and RNA aligns it with the nucleic acid-binding properties of the translin protein family, known for its roles in DNA repair, RNA metabolism, and mRNA transport. We report for the first time the presence of a translin-like protein that forms octameric rings, is more closely related to rice translin, and is localized to an organelle not yet known to harbor such a family of proteins, viz., in the basal body and flagella of C. reinhardtii. This study lays the groundwork for future investigations into the molecular functions of Crtranslin and its potential regulatory roles in flagellar dynamics. Impact statement This is the first report of the presence of a nucleic acid-binding protein, Translin, in the basal body and cilia.

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Publication Details

Journal
FEBS Letters
Published
2026-02-06
DOI
https://doi.org/10.1002/1873-3468.70289
Primary Topic
Microtubule and mitosis dynamics
Type
article
Field-Weighted Citation Impact
0.00

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article

Characterization of a nucleic acid‐binding translin‐like protein localized to the basal body in the unicellular green alga Chlamydomonas reinhardtii

Dhruv Das, Rajani Kant Chittela, Saptadipa Basak, Hanee Arkate et al.
FEBS Letters
Microtubule and mitosis dynamics
article

Characterization of a nucleic acid‐binding translin‐like protein localized to the basal body in the unicellular green alga Chlamydomonas reinhardtii

Dhruv Das, Rajani Kant Chittela, Saptadipa Basak, Hanee Arkate, Jacinta S D'Souza
article en

Abstract

This study characterizes a translin-like protein from Chlamydomonas reinhardtii, a unicellular alga. The efficient binding of the Crtranslin protein to both single-stranded DNA and RNA aligns it with the nucleic acid-binding properties of the translin protein family, known for its roles in DNA repair, RNA metabolism, and mRNA transport. We report for the first time the presence of a translin-like protein that forms octameric rings, is more closely related to rice translin, and is localized to an organelle not yet known to harbor such a family of proteins, viz., in the basal body and flagella of C. reinhardtii. This study lays the groundwork for future investigations into the molecular functions of Crtranslin and its potential regulatory roles in flagellar dynamics. Impact statement This is the first report of the presence of a nucleic acid-binding protein, Translin, in the basal body and cilia.

FEBS Letters
Bhabha Atomic Research Centre (IN), Homi Bhabha National Institute (IN), Department of Atomic Energy (IN), Bhabha Atomic Research Center Hospital (IN), Center for Excellence in Basic Sciences (IN)
Bhabha Atomic Research Centre, Tata Memorial Centre
Life in Land
Openalex Percentile: Top 68%
Microtubule and mitosis dynamics
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Characterization of a nucleic acid‐binding translin‐like protein localized to the basal body in the unicellular green alga <i>Chlamydomonas reinhardtii</i> — Dhruv Das, Rajani Kant Chittela, et al. · FEBS Letters (2026) | TGRS Research Map | TGRS