Abstract
We found 33, 17, and 20 Alba genes in Gossypium hirsutum, Gossypium arboretum, and Gossypium raimondii, respectively. The Alba protein lengths ranged from 62 to 312 aa, the molecular weight (MW) from 7.003 to 34.55 kDa, grand average hydropathy values of −1.012 to 0.609 and isoelectric (pI) values of −3 to 11. Moreover, miRNAs such as gra-miR8770 targeted four genes, gra-miR8752 and gra-miR8666 targeted three genes, and each and gra-miR8657 a, b, c, d, e targeted 10 genes each, while the rests targeted 1 to 2 genes each. Similarly, various cis-regulatory elements were detected with significant roles in enhancing abiotic stress tolerance, such as CBFHV (RYCGAC) with a role in cold stress acclimation among others. Two genes, Gh_D01G0884 and Gh_D01G0922, were found to be highly induced under water deficit and salt stress conditions. Through virus-induced gene silencing (VIGS), the VIGS cotton plants were found to be highly susceptible to both water deficit and salt stresses; the VIGS plants exhibited a significant reduction in root growth, low cell membrane stability (CMS), saturated leaf weight (SLW), chlorophyll content levels, and higher excised leaf water loss (ELWL). Furthermore, the stress-responsive genes and ROS scavenging enzymes were significantly reduced in the VIGS plants compared to either the wild type (WT) and or the positively controlled plants. The VIGS plants registered higher concentration levels of hydrogen peroxide and malondialdehyde, with significantly lower levels of the various antioxidants evaluated an indication that the VIGS plants were highly affected by salt and drought stresses. This result provides a key foundation for future exploration of the Alba proteins in relation to abiotic stress.
Highlights
acetylation lower binding affinity (Alba) family proteins are mainly referred to as basic, small, and dimeric nucleic acid-binding proteins and are mainly distributed in a number of eukaryotes and the archaeal organisms (Subota et al, 2011)
The Alba proteins for G. hirsutum AD genome, G. arboreum of A genome, and G. raimondii of the D genome [together with the whole sequences for Arabidopsis thaliana obtained from TAIR], O. sativa obtained from http://rice.plantbiology.msu.edu/index.shtml, Theobroma cacao, Sorghum bicolor, Glycine max, and Populus trichocarpa were all downloaded from Phytozome v12.0 and were used to investigate the evolutionary relationships of the Alba proteins in plants (Table S1)
A total of 33, 20, and 17 proteins encoded by the Alba genes were identified in G. hirsutum, G. raimondii, and G. arboreum, respectively
Summary
Alba family proteins are mainly referred to as basic, small, and dimeric nucleic acid-binding proteins and are mainly distributed in a number of eukaryotes and the archaeal organisms (Subota et al, 2011). Knockdown of Novel Alba Genes have a distinctive property in the regulation and organization of the organism’s genomes through acetylation and deacetylation (Goyal et al, 2012). Apart from the acetylation at the N-terminal of the lysine residues, the Alba proteins contain arginine–glycine–glycine (RGG) repeat at the C-terminal, which are important mediators of protein:RNA, and protein: protein interactions resulting in the formation of the membraneless ribonucleoprotein granules (Chong et al, 2018). The RGG domain, are closely spaced arginine–glycine–glycine repeats, it is a DNA and RNA-binding domain in various nucleic acid-binding proteins (Arribas-Layton et al, 2016). Structural analysis of the Alba proteins reveals the homodimer (dimeric) nature of the proteins (Bell et al, 2002)
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