A family portrait: structural comparison of the Whirly proteins from<i>Arabidopsis thaliana</i>and<i>Solanum tuberosum</i>

Cappadocia, Laurent; Parent, Jean-Sébastien; Sygusch, J.; Brisson, Normand

doi:10.1107/s1744309113028698

Cited by 15 publications

(19 citation statements)

References 18 publications

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“…In chloroplasts, WHY1 were found to associate with nucleoids [ 14 , 15 , 47 ], but only a minor part of WHY1 colocalizes with cp nucleoids that was showed by high-resolution imaging [ 48 ]. The elusive and complex localization of WHIRLY may represent its multifunctionality.…”

Section: Discussionmentioning

confidence: 99%

Dual-Located WHIRLY1 Interacting with LHCA1 Alters Photochemical Activities of Photosystem I and Is Involved in Light Adaptation in Arabidopsis

Huang

Lin

Deng

et al. 2017

IJMS

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Plastid-nucleus-located WHIRLY1 protein plays a role in regulating leaf senescence and is believed to associate with the increase of reactive oxygen species delivered from redox state of the photosynthetic electron transport chain. In order to make sure whether WHIRLY1 plays a role in photosynthesis, in this study, the performances of photosynthesis were detected in Arabidopsis whirly1 knockout (kowhy1) and plastid localized WHIRLY1 overexpression (oepWHY1) plants. Loss of WHIRLY1 leads to a higher photochemical quantum yield of photosystem I Y(I) and electron transport rate (ETR) and a lower non-photochemical quenching (NPQ) involved in the thermal dissipation of excitation energy of chlorophyll fluorescence than the wild type. Further analyses showed that WHIRLY1 interacts with Light-harvesting protein complex I (LHCA1) and affects the expression of genes encoding photosystem I (PSI) and light harvest complexes (LHCI). Moreover, loss of WHIRLY1 decreases chloroplast NAD(P)H dehydrogenase-like complex (NDH) activity and the accumulation of NDH supercomplex. Several genes encoding the PSI-NDH complexes are also up-regulated in kowhy1 and the whirly1whirly3 double mutant (ko1/3) but steady in oepWHY1 plants. However, under high light conditions (800 μmol m−2 s−1), both kowhy1 and ko1/3 plants show lower ETR than wild-type which are contrary to that under normal light condition. Moreover, the expression of several PSI-NDH encoding genes and ERF109 which is related to jasmonate (JA) response varied in kowhy1 under different light conditions. These results indicate that WHIRLY1 is involved in the alteration of ETR by affecting the activities of PSI and supercomplex formation of PSI with LHCI or NDH and may acting as a communicator between the plastids and the nucleus.

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Section: Discussionmentioning

confidence: 99%

Dual-Located WHIRLY1 Interacting with LHCA1 Alters Photochemical Activities of Photosystem I and Is Involved in Light Adaptation in Arabidopsis

Huang

Lin

Deng

et al. 2017

IJMS

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“…The closest structural homolog, as determined using the DALI server (Holm et al, 2008), is a mitochondrial Whirly protein (Why2; PDB entry 4kop) from Arabidopsis thaliana (Cappadocia et al, 2013), and CdiI o2 MC58-1 superimposes upon Why2 with an r.m.s.d. of 2.5 Å over 80 of 145 C atoms (Figs.…”

Section: O2mentioning

confidence: 99%

“…MC58-1 has moderate structural similarity to two eukaryotic nucleic acid-binding proteins. The closest structural homolog, as determined using the DALI server (Holm et al, 2008), is a mitochondrial Whirly protein (Why2; PDB entry 4kop) from Arabidopsis thaliana (Cappadocia et al, 2013), and CdiI o2…”

Section: O2mentioning

confidence: 99%

The structure of a contact-dependent growth-inhibition (CDI) immunity protein fromNeisseria meningitidisMC58

et al. 2015

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Contact-dependent growth inhibition (CDI) is an important mechanism of intercellular competition between neighboring Gram-negative bacteria. CDI systems encode large surface-exposed CdiA effector proteins that carry a variety of C-terminal toxin domains (CdiA-CTs). All CDI + bacteria also produce CdiI immunity proteins that specifically bind to the cognate CdiA-CT and neutralize its toxin activity to prevent auto-inhibition. Here, the X-ray crystal structure of a CdiI immunity protein from Neisseria meningitidis MC58 is presented at 1.45 Å resolution. The CdiI protein has structural homology to the Whirly family of RNA-binding proteins, but appears to lack the characteristic nucleic acid-binding motif of this family. Sequence homology suggests that the cognate CdiA-CT is related to the eukaryotic EndoU family of RNA-processing enzymes. A homology model is presented of the CdiA-CT based on the structure of the XendoU nuclease from Xenopus laevis. Molecular-docking simulations predict that the CdiA-CT toxin active site is occluded upon binding to the CdiI immunity protein. Together, these observations suggest that the immunity protein neutralizes toxin activity by preventing access to RNA substrates.

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“…As a single-stranded DNA binding protein, WHIRLY domains are four structural topologies that have been structurally characterized with ssDNA ( Dickey et al, 2013 ). WHIRLY domains are approximately 180-amino-acid-long domains characterized by two roughly parallel four-stranded β sheets with interspersed helical elements ( Desveaux et al, 2005 ; Cappadocia et al, 2013 ).…”

Section: Introductionmentioning

confidence: 99%

WHIRLY1 Occupancy Affects Histone Lysine Modification and WRKY53 Transcription in Arabidopsis Developmental Manner

Huang

Lan

et al. 2018

Front. Plant Sci.

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Single-stranded DNA-binding proteins (SSBs) are assumed to involve in DNA replication, DNA repairmen, and gene transcription. Here, we provide the direct evidence on the functionality of an Arabidopsis SSB, WHIRLY1, by using loss- or gain-of-function lines. We show that WHIRLY1 binding to the promoter of WRKY53 represses the enrichment of H3K4me3, but enhances the enrichment of H3K9ac at the region contained WHIRLY1-binding sequences and TATA box or the translation start region of WRKY53, coincided with a recruitment of RNAPII. In vitro ChIP assays confirm that WHIRLY1 inhibits H3K4me3 enrichment at the preinitiation complex formation stage, while promotes H3K9ac enrichment and RNAPII recruitment at the elongation stage, consequently affecting the transcription of WRKY53. These results further explore the molecular actions underlying SSB-mediated gene transcription through epigenetic regulation in plant senescence.

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A family portrait: structural comparison of the Whirly proteins fromArabidopsis thalianaandSolanum tuberosum

Cited by 15 publications

References 18 publications

Dual-Located WHIRLY1 Interacting with LHCA1 Alters Photochemical Activities of Photosystem I and Is Involved in Light Adaptation in Arabidopsis

Dual-Located WHIRLY1 Interacting with LHCA1 Alters Photochemical Activities of Photosystem I and Is Involved in Light Adaptation in Arabidopsis

The structure of a contact-dependent growth-inhibition (CDI) immunity protein fromNeisseria meningitidisMC58

WHIRLY1 Occupancy Affects Histone Lysine Modification and WRKY53 Transcription in Arabidopsis Developmental Manner

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