Impact of Genome Reduction in Microsporidia

Jespersen, Nathan; Barandun, Jonas

doi:10.1007/978-3-030-93306-7_1

Cited by 25 publications

(39 citation statements)

References 184 publications

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“…Our analysis suggests that this evolutionary transformation is primarily caused by changes in the msL1/msL2 ribosomal binding site. This finding is consistent with previous studies showing that microsporidian rRNA appears to evolve faster than microsporidian ribosomal proteins (34)(35)(36)(37)(38)(39)(40)(41)(42)(43). It is, therefore, possible that microsporidian ribosomal proteins are frequently required to adapt to rRNA variations to compensate for rRNA variations.…”

Section: In Non-globular Proteins Structure Can Evolve Faster Than Se...supporting

confidence: 92%

A conserved ribosomal protein has entirely dissimilar structures in different organisms

Schierholz

Brown

Helena-Bueno

et al. 2022

Preprint

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It is generally accepted that protein structures are more conserved than protein sequences. This notion is widely used to identify distant protein homologs and predict the structure and functions of uncharacterized proteins. However, this principle has been derived from studies of globular proteins, leaving it unclear whether the same principle is applied to non-globular (or intrinsically disordered) proteins. Here, to help answer this question, we describe the evolution of the ribosomal protein msL1/msL2 that was recently found in ribosomes from the parasitic microorganisms microsporidia. We first show that this protein has conserved function but entirely dissimilar structures in different organisms: in each of the analyzed species, msL1/msL2 exhibits an altered secondary structure, an inverted orientation of the N- and C-termini, and a completely transformed fold. We then show that this fold change is likely caused by the evolution of the msL1/msL2-binding site in the ribosome; specifically, by variations in microsporidian rRNA. These findings illustrate that structure may evolve faster than sequence in non-globular proteins. Hence, non-globular proteins can completely transform their fold without loss of function, challenging the current sequence-structure-function paradigm that is viewed as a universal principle of protein evolution.

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Section: In Non-globular Proteins Structure Can Evolve Faster Than Se...supporting

confidence: 92%

A conserved ribosomal protein has entirely dissimilar structures in different organisms

Schierholz

Brown

Helena-Bueno

et al. 2022

Preprint

Self Cite

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“…The phylogenetic tree generated using high-confidence proteasomal subunits ( Fig. 6a ) is consistent with trees derived from simplified rRNA or whole-proteome analyses 3,51 . Saliently, a comparison of the relative length and conservation of proteasomal subunits between microsporidia and selected eukaryotes to S. cerevisiae reveals widespread evidence of reductive evolution ( Fig.…”

Section: Resultssupporting

confidence: 69%

“…Indeed, two evolutionarily adjacent Nematocida spp. share only ∼68% of their sequence 48 , and even in complexes as universally conserved as ribosomes, yeast and microsporidian homologs are only 38% identical in sequence on average 3 . This sequence diversity confounds not only phylogenetic classification, but also attempts to identify microsporidian homologs, which hampers our functional understanding of these ecologically important organisms.…”

Section: Resultsmentioning

confidence: 99%

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Reductive evolution in the structure of the microsporidian proteasome

Jespersen

Ehrenbolger

Winiger

et al. 2022

Preprint

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Proteasomes play an essential role in the life cycle of intracellular pathogens with extracellular stages by ensuring proteostasis in environments with limited resources. In microsporidia, divergent parasites with extraordinarily streamlined genomes, the proteasome complexity and structure are unknown, which limits our understanding of how these unique pathogens adapt and compact essential eukaryotic complexes. We present cryo-electron microscopy structures of the microsporidian 20S and 26S proteasome isolated from dormant or germinated Vairimorpha necatrix spores. The presence of distinct densities within the central cavity of the dormant spore proteasome suggests reduced activity in the environmental stage. In contrast, the absence of these densities and the existence of 26S particles post-germination indicates rapid reactivation of proteasomes after host infection. Structual and phylogenetic analyses reveal that microsporidian proteasomes have undergone extreme reductive evolution, lost three regulatory proteins, and compacted nearly every subunit. The highly derived microsporidian proteasome structure presented here reinforces the feasibility of the development of specific inhibitors and provides insight into the unique evolution and biology of these medically and economically important pathogens.

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“…The discovery potential is enormous and can be easily illustrated by recent studies on ribosomal structures of parasitic ribosomal subunits that revealed how reductive evolution may shape ribosome biogenesis and function. Moreover, unleashing these ‘new worlds’ will also open a window towards better understanding of major evolutionary constraints of ribosome synthesis and function [ 9 , 14 , 15 , 60 , 73 , 76 ].…”

Section: New World Unleashedmentioning

confidence: 99%

The dark side of the ribosome life cycle

Ferreira-Cerca

2022

RNA Biology

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Thanks to genetics, biochemistry, and structural biology many features of the ribosome´s life cycles in models of bacteria, eukaryotes, and some organelles have been revealed to near-atomic details. Collectively, these studies have provided a very detailed understanding of what are now well-established prototypes for ribosome biogenesis and function as viewed from a ‘classical’ model organisms perspective. However, very important challenges remain ahead to explore the functional and structural diversity of both ribosome biogenesis and function across the biological diversity on earth. Particularly, the ‘third domain of life’, the archaea, and also many non-model bacterial and eukaryotic organisms have been comparatively neglected. Importantly, characterizing these additional biological systems will not only offer a yet untapped window to enlighten the evolution of ribosome biogenesis and function but will also help to unravel fundamental principles of molecular adaptation of these central cellular processes.

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Impact of Genome Reduction in Microsporidia

Cited by 25 publications

References 184 publications

A conserved ribosomal protein has entirely dissimilar structures in different organisms

A conserved ribosomal protein has entirely dissimilar structures in different organisms

Reductive evolution in the structure of the microsporidian proteasome

The dark side of the ribosome life cycle

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