scholarly journals Reductive evolution of architectural repertoires in proteomes and the birth of the tripartite world

2007 ◽  
Vol 17 (11) ◽  
pp. 1572-1585 ◽  
Author(s):  
M. Wang ◽  
L. S. Yafremava ◽  
D. Caetano-Anolles ◽  
J. E. Mittenthal ◽  
G. Caetano-Anolles
Keyword(s):  
Biomolecules ◽  
2020 ◽  
Vol 10 (4) ◽  
pp. 587
Author(s):  
Pascal Sirand-Pugnet ◽  
Damien Brégeon ◽  
Laure Béven ◽  
Catherine Goyenvalle ◽  
Alain Blanchard ◽  
...  

The C5-methylation of uracil to form 5-methyluracil (m5U) is a ubiquitous base modification of nucleic acids. Four enzyme families have converged to catalyze this methylation using different chemical solutions. Here, we investigate the evolution of 5-methyluracil synthase families in Mollicutes, a class of bacteria that has undergone extensive genome erosion. Many mollicutes have lost some of the m5U methyltransferases present in their common ancestor. Cases of duplication and subsequent shift of function are also described. For example, most members of the Spiroplasma subgroup use the ancestral tetrahydrofolate-dependent TrmFO enzyme to catalyze the formation of m5U54 in tRNA, while a TrmFO paralog (termed RlmFO) is responsible for m5U1939 formation in 23S rRNA. RlmFO has replaced the S-adenosyl-L-methionine (SAM)-enzyme RlmD that adds the same modification in the ancestor and which is still present in mollicutes from the Hominis subgroup. Another paralog of this family, the TrmFO-like protein, has a yet unidentified function that differs from the TrmFO and RlmFO homologs. Despite having evolved towards minimal genomes, the mollicutes possess a repertoire of m5U-modifying enzymes that is highly dynamic and has undergone horizontal transfer.


2014 ◽  
Vol 42 (6) ◽  
pp. 1734-1739 ◽  
Author(s):  
Michael L. Ginger

Reductive evolution during the adaptation to obligate parasitism and expansions of gene families encoding virulence factors are characteristics evident to greater or lesser degrees in all parasitic protists studied to date. Large evolutionary distances separate many parasitic protists from the yeast and animal models upon which classic views of eukaryotic biochemistry are often based. Thus a combination of evolutionary divergence, niche adaptation and reductive evolution means the biochemistry of parasitic protists is often very different from their hosts and to other eukaryotes generally, making parasites intriguing subjects for those interested in the phenomenon of moonlighting proteins. In common with other organisms, the contribution of protein moonlighting to parasite biology is only just emerging, and it is not without controversy. Here, an overview of recently identified moonlighting proteins in parasitic protists is provided, together with discussion of some of the controversies.


Parasitology ◽  
2018 ◽  
Vol 145 (10) ◽  
pp. 1311-1323 ◽  
Author(s):  
Jane Harmer ◽  
Vyacheslav Yurchenko ◽  
Anna Nenarokova ◽  
Julius Lukeš ◽  
Michael L. Ginger

AbstractParasitic trypanosomatids diverged from free-living kinetoplastid ancestors several hundred million years ago. These parasites are relatively well known, due in part to several unusual cell biological and molecular traits and in part to the significance of a few – pathogenic Leishmania and Trypanosoma species – as aetiological agents of serious neglected tropical diseases. However, the majority of trypanosomatid biodiversity is represented by osmotrophic monoxenous parasites of insects. In two lineages, novymonads and strigomonads, osmotrophic lifestyles are supported by cytoplasmic endosymbionts, providing hosts with macromolecular precursors and vitamins. Here we discuss the two independent origins of endosymbiosis within trypanosomatids and subsequently different evolutionary trajectories that see entrainment vs tolerance of symbiont cell divisions cycles within those of the host. With the potential to inform on the transition to obligate parasitism in the trypanosomatids, interest in the biology and ecology of free-living, phagotrophic kinetoplastids is beginning to enjoy a renaissance. Thus, we take the opportunity to additionally consider the wider relevance of endosymbiosis during kinetoplastid evolution, including the indulged lifestyle and reductive evolution of basal kinetoplastid Perkinsela.


2006 ◽  
Vol 103 (24) ◽  
pp. 9274-9279 ◽  
Author(s):  
M. van de Guchte ◽  
S. Penaud ◽  
C. Grimaldi ◽  
V. Barbe ◽  
K. Bryson ◽  
...  

Author(s):  
J. Tze-Fei Wong ◽  
Xi Long ◽  
Hong Xue

AbstractThe findings of a deep branching Microsporidia clade on the SSU rRNA tree, and diversity of sequence motifs in eukaryotic Hsp70s rendered invalid the endosymbiosis-first theory that mitosome- and hydrogenosome-containing amitochondriate eukaryotes (AMIs) arose from mitochondriate eukaryotes (MTEs) via reductive evolution. Instead, evidence of widespread ectosymbioses indicated that eukaryogenesis was started by an archaeal parent via its acquisition of archaeal proteins through ‘accelerated gene adoption’, and bacterial proteins from ectosymbionts including a clostridial ectosymbiont that supplied its [Fe] hydrogenase and pyruvate:ferredoxin oxidoreductase genes to the AMIs. Subsequent endosymbiosis with Tistrella gave rise to mitochondria with the participation of other alphaproteobacteria. The high frequencies of top similarity bitscores displayed by Giardia, Edhazardia and Trichomonas toward Aciduliprofundum boonei (Abo) pertaining to the enzymes of DNA biology, far surpassing the frequencies toward any Asgard or TACK archaeon, established Abo as the source of these enzymes in eukaryotes, and the archaeal parent of Eukarya.


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