scholarly journals Elucidating the evolutionary history and expression patterns of nucleoside phosphorylase paralogs (vegetative storage proteins) in Populus and the plant kingdom

2013 ◽  
Vol 13 (1) ◽  
pp. 118 ◽  
Author(s):  
Emily A Pettengill ◽  
James B Pettengill ◽  
Gary D Coleman
2019 ◽  
Vol 286 (1897) ◽  
pp. 20182929 ◽  
Author(s):  
Elena A. Ritschard ◽  
Robert R. Fitak ◽  
Oleg Simakov ◽  
Sönke Johnsen

Coleoid cephalopods show unique morphological and neural novelties, such as arms with tactile and chemosensory suckers and a large complex nervous system. The evolution of such cephalopod novelties has been attributed at a genomic level to independent gene family expansions, yet the exact association and the evolutionary timing remain unclear. In the octopus genome, one such expansion occurred in the G-protein-coupled receptors (GPCRs) repertoire, a superfamily of proteins that mediate signal transduction. Here, we assessed the evolutionary history of this expansion and its relationship with cephalopod novelties. Using phylogenetic analyses, at least two cephalopod- and two octopus-specific GPCR expansions were identified. Signatures of positive selection were analysed within the four groups, and the locations of these sequences in the Octopus bimaculoides genome were inspected. Additionally, the expression profiles of cephalopod GPCRs across various tissues were extracted from available transcriptomic data. Our results reveal the evolutionary history of cephalopod GPCRs. Unexpanded cephalopod GPCRs shared with other bilaterians were found to be mainly nervous tissue specific. By contrast, duplications that are shared between octopus and the bobtail squid or specific to the octopus' lineage generated copies with divergent expression patterns devoted to tissues outside of the brain. The acquisition of novel expression domains was accompanied by gene order rearrangement through either translocation or duplication and gene loss. Lastly, expansions showed signs of positive selection and some were found to form tandem clusters with shared conserved expression profiles in cephalopod innovations such as the axial nerve cord. Altogether, our results contribute to the understanding of the molecular and evolutionary history of signal transduction and provide insights into the role of this expansion during the emergence of cephalopod novelties and/or adaptations.


2005 ◽  
Vol 32 (4) ◽  
pp. 335 ◽  
Author(s):  
Kimberly A. Murphy ◽  
Rachel A. Kuhle ◽  
Andreas M. Fischer ◽  
Aldwin M. Anterola ◽  
Howard D. Grimes

Antibodies raised against tonoplast intrinsic proteins (TIPs) were used to probe the functional status of the soybean [Glycine max (L.) Merr.] paraveinal mesophyll (PVM) vacuole during changes in nitrogen metabolism within the leaf. Young plants grown under standard conditions had PVM vacuoles characterised by the presence of γ-TIP, which is indicative of a lytic function. When plants were then subjected to shoot tip removal for a period of 15 d, forcing a sink-limited physiological condition, the γ-TIP marker diminished while the δ-TIP marker became present in the PVM vacuole, indicating the conversion of the PVM vacuole to a storage function. When the shoot tips were allowed to regrow, the γ-TIP marker again became dominant demonstrating the reversion of these PVM vacuoles back to a lytic compartment. The changes in TIP markers correlated with the accumulation of vegetative storage proteins and vegetative lipoxygenases, proteins implicated in nitrogen storage and assimilate partitioning. This research suggests that the PVM vacuole is able to undergo dynamic conversion between lytic and storage functions and further implicates this cell layer in assimilate storage and mobilisation in soybeans.


IAWA Journal ◽  
2003 ◽  
Vol 24 (4) ◽  
pp. 421-428
Author(s):  
Wei-Min Tian ◽  
Zheng-Hai Hu

The distribution pattern of vegetative storage proteins is reported for the first time for 18 species and 2 varieties of twelve genera of Rosaceae. Vegetative storage proteins were present in all the species studied of Prunoideae and absent in Maloideae. Their occurrence in a genus seemed to be either universal or entirely absent. Rosaceae trees were poor in vegetative storage proteins and the form of vegetative storage proteins was not protein body-like. Granular and floccular forms of vegetative storage proteins could be distinguished exclusively in the secondary phloem parenchyma cells and their distribution was cell-specific. Our results suggest that the distribution of vegetative storage proteins in Rosaceae can be considered as a taxonomically diagnostic feature. The nature of the bark proteins with seasonal changes in apple trees is discussed.


2011 ◽  
Vol 279 (1726) ◽  
pp. 3-14 ◽  
Author(s):  
Megan L. Porter ◽  
Joseph R. Blasic ◽  
Michael J. Bok ◽  
Evan G. Cameron ◽  
Thomas Pringle ◽  
...  

Opsin proteins are essential molecules in mediating the ability of animals to detect and use light for diverse biological functions. Therefore, understanding the evolutionary history of opsins is key to understanding the evolution of light detection and photoreception in animals. As genomic data have appeared and rapidly expanded in quantity, it has become possible to analyse opsins that functionally and histologically are less well characterized, and thus to examine opsin evolution strictly from a genetic perspective. We have incorporated these new data into a large-scale, genome-based analysis of opsin evolution. We use an extensive phylogeny of currently known opsin sequence diversity as a foundation for examining the evolutionary distributions of key functional features within the opsin clade. This new analysis illustrates the lability of opsin protein-expression patterns, site-specific functionality (i.e. counterion position) and G-protein binding interactions. Further, it demonstrates the limitations of current model organisms, and highlights the need for further characterization of many of the opsin sequence groups with unknown function.


2002 ◽  
Vol 80 (4) ◽  
pp. 321-329 ◽  
Author(s):  
J Derek Bewley

The presence of storage proteins has been reported in roots of several perennial and biennial weed and crop species, and particularly in members of the Compositae, Euphorbiaceae, and Leguminosae. In some species the amount of these root proteins fluctuates seasonally, increasing in the fall and winter months and declining in the spring and early summer. Also, the root proteins may decline during regrowth of decapitated plants. The evidence that these proteins play a role as storage proteins is frequently only circumstantial; moreover, they are usually only a relatively minor component of the total nitrogen pool within the root. Only one root protein, that from the dandelion taproot, has been extensively characterized, and it has no properties in common with known vegetative storage proteins. The literature on root proteins is reviewed, with particular emphasis on those present in taproots. The paucity of definitive data allows few conclusions to be reached, and more research is required to establish the role, nature, and importance of root proteins.Key words: taproots, perennial weeds, root proteins, nitrogen pools, storage proteins.


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