WHIRLY1 is a major organizer of chloroplast nucleoids

Krupinska, Karin; Oetke, Svenja; Desel, Christine; Mulisch, Maria; Schäfer, Anke; Hollmann, Julien; Kumlehn, Jochen; Hensel, Goetz

doi:10.3389/fpls.2014.00432

Cited by 50 publications

(103 citation statements)

References 55 publications

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“…The transcript profile analysis of the WHIRLYdeficient leaves showed that genes encoding discrete subsets of photosynthetic proteins were markedly changed relative to the wild type. These findings are consistent with the observation that barley leaves seem to be less able to regulate cpDNA copy number in the absence of WHIRLY1 (Krupinska et al, 2014b). Transcripts encoding photosynthetic proteins, including the thylakoid NADH dehydrogenase and cytochrome b/f complexes, and chloroplast ribosomes were more abundant in the WHIRLY-deficient leaves than the wild type.…”

Section: Discussionsupporting

confidence: 90%

“…This transcript is identical to the barley organelle DNA polymerase described recently (Krupinska et al, 2014a(Krupinska et al, , 2014b and homologous to the AtPol1B (At3g20540) sequence. Similarly, a microtubule end binding protein 1A (MLOC 52339.1) and a transcript encoding a protein containing a B3 DNA binding domain (AK251585.1) that is found exclusively in transcription factors were significantly more abundant in W1-7 leaves relative to the wild type ( Fig.…”

Section: The Transcript Profile Is Modified In Whirly1-deficient Leavessupporting

confidence: 58%

“…Line W1-7 has no detectable WHIRLY1 protein and has already been characterized in terms of cpDNA content and nucleoid structure (Krupinska et al, 2014b). We, therefore, performed a more in-depth analysis on the physiology, transcriptome, and metabolome profiles of line W1-7 at the early stages of leaf development.…”

Section: The Phenotype Of Whirly1-deficient Barley Seedlingsmentioning

confidence: 99%

“…Although early studies indicated that WHIRLY1 did not associate with plastid nucleoids (Melonek et al, 2010), loss of the WHIRLY1 protein resulted in a slight increase in cpDNA copy number, correlating with increased expression of an organellar DNA polymerase (Krupinska et al, 2014b). Recent evidence from studies using a recombinant form of WHIRLY1 suggested that the protein could translocate from transplastomic chloroplasts to the nucleus (Isemer et al, 2012b).…”

mentioning

confidence: 99%

“…A better understanding of the inherent adaptive responses of plants to low-nitrogen availability is, therefore, required to improve nitrogen use efficiency and maintain high productivity on reduced nitrogen inputs. In the following studies, therefore, we have explored the functions of WHIRLY1 in chloroplasts using transgenic barley lines (WHIRLY1-1 [W1-1], W1-7, and W1-9) that have only about 5% or less of the wild-type WHIRLY1 protein (Melonek et al, 2010;Krupinska et al, 2014b) under different growth nitrogen regimes. We present data showing that the WHIRLY1 protein influences the expression of specific subsets of transcripts encoding chloroplast proteins, resulting in a reduced sensitivity of photosynthesis to low nitrogen.…”

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confidence: 99%

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WHIRLY1 Functions in the Control of Responses to Nitrogen Deficiency But Not Aphid Infestation in Barley

et al. 2015

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WHIRLY1 is largely targeted to plastids, where it is a major constituent of the nucleoids. To explore WHIRLY1 functions in barley (Hordeum vulgare), RNA interference-knockdown lines (W1-1, W1-7, and W1-9) that have very low levels of HvWHIRLY1 transcripts were characterized in plants grown under optimal and stress conditions. The WHIRLY1-1 (W1-1), W1-7, and W1-9 plants were phenotypically similar to the wild type but produced fewer tillers and seeds. Photosynthesis rates were similar in all lines, but W1-1, W1-7, and W1-9 leaves had significantly more chlorophyll and less sucrose than the wild type. Transcripts encoding specific subsets of chloroplast-localized proteins, such as ribosomal proteins, subunits of the RNA polymerase, and thylakoid nicotinamide adenine dinucleotide (reduced) and cytochrome b 6 /f complexes, were much more abundant in the W1-7 leaves than the wild type. Although susceptibility of aphid (Myzus persicae) infestation was similar in all lines, the WHIRLY1-deficient plants showed altered responses to nitrogen deficiency, maintaining higher photosynthetic CO 2 assimilation rates than the wild type under limiting nitrogen. Although all lines showed globally similar low nitrogen-dependent changes in transcripts and metabolites, the increased abundance of FAR-RED IMPAIRED RESPONSE1-like transcripts in nitrogen-deficient W1-7 leaves infers that WHIRLY1 has a role in communication between plastid and nuclear genes encoding photosynthetic proteins during abiotic stress.

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Section: Discussionsupporting

confidence: 90%

Section: The Transcript Profile Is Modified In Whirly1-deficient Leavessupporting

confidence: 58%

Section: The Phenotype Of Whirly1-deficient Barley Seedlingsmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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WHIRLY1 Functions in the Control of Responses to Nitrogen Deficiency But Not Aphid Infestation in Barley

et al. 2015

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WHIRLY protein functions in plants

Taylor

West

Foyer

2022

Food and Energy Security

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Environmental stresses pose a significant threat to food security. Understanding the function of proteins that regulate plant responses to biotic and abiotic stresses is therefore pivotal in developing strategies for crop improvement. The WHIRLY (WHY) family of DNA‐binding proteins are important in this regard because they fulfil a portfolio of important functions in organelles and nuclei. The WHY1 and WHY2 proteins function as transcription factors in the nucleus regulating phytohormone synthesis and associated growth and stress responses, as well as fulfilling crucial roles in DNA and RNA metabolism in plastids and mitochondria. WHY1, WHY2 (and WHY3 proteins in Arabidopsis) maintain organelle genome stability and serve as auxiliary factors for homologous recombination and double‐strand break repair. Our understanding of WHY protein functions has greatly increased in recent years, as has our knowledge of the flexibility of their localization and overlap of functions but there is no review of the topic in the literature. Our aim in this review was therefore to provide a comprehensive overview of the topic, discussing WHY protein functions in nuclei and organelles and highlighting roles in plant development and stress responses. In particular, we consider areas of uncertainty such as the flexible localization of WHY proteins in terms of retrograde signalling connecting mitochondria, plastids, and the nucleus. Moreover, we identify WHY proteins as important targets in plant breeding programmes designed to increase stress tolerance and the sustainability of crop yield in a changing climate.

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WHIRLY2 plays a key role in mitochondria morphology, dynamics, and functionality in Arabidopsis thaliana

et al. 2020

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WHIRLY2 is a single‐stranded DNA binding protein associated with mitochondrial nucleoids. In the why 2‐1 mutant of Arabidopsis thaliana, a major proportion of leaf mitochondria has an aberrant structure characterized by disorganized nucleoids, reduced abundance of cristae, and a low matrix density despite the fact that the macroscopic phenotype during vegetative growth is not different from wild type. These features coincide with an impairment of the functionality and dynamics of mitochondria that have been characterized in detail in wild‐type and why 2‐1 mutant cell cultures. In contrast to the development of the vegetative parts, seed germination is compromised in the why 2‐1 mutant. In line with that, the expression level of why 2 in seeds of wild‐type plants is higher than that of why 3, whereas in adult plant no difference is found. Intriguingly, in early stages of shoots development of the why 2‐1 mutant, although not in seeds, the expression level of why 3 is enhanced. These results suggest that WHIRLY3 is a potential candidate to compensate for the lack of WHIRLY2 in the why 2‐1 mutant. Such compensation is possible only if the two proteins are localized in the same organelle. Indeed, in organello protein transport experiments using intact mitochondria and chloroplasts revealed that WHIRLY3 can be dually targeted into both, chloroplasts and mitochondria. Together, these data indicate that the alterations of mitochondria nucleoids are tightly linked to alterations of mitochondria morphology and functionality. This is even more evident in those phases of plant life when mitochondrial activity is particularly high, such as seed germination. Moreover, our results indicate that the differential expression of why 2 and why 3 predetermines the functional replacement of WHIRLY2 by WHIRLY3, which is restricted though to the vegetative parts of the plant.

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WHIRLY1 is a major organizer of chloroplast nucleoids

Cited by 50 publications

References 55 publications

WHIRLY1 Functions in the Control of Responses to Nitrogen Deficiency But Not Aphid Infestation in Barley

WHIRLY1 Functions in the Control of Responses to Nitrogen Deficiency But Not Aphid Infestation in Barley

WHIRLY protein functions in plants

WHIRLY2 plays a key role in mitochondria morphology, dynamics, and functionality in Arabidopsis thaliana

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