Molecular characterization and evolutionary origins of farinin genes in Brachypodium distachyon L.

Manzoor

et al. 2022

IJMS

The SAUR (small auxin-up RNA) gene family is the biggest family of early auxin response genes in higher plants and has been associated with the control of a variety of biological processes. Although SAUR genes had been identified in several genomes, no systematic analysis of the SAUR gene family has been reported in Chinese white pear. In this study, comparative and systematic genomic analysis has been performed in the SAUR gene family and identified a total of 116 genes from the Chinese white pear. A phylogeny analysis revealed that the SAUR family could be classified into four groups. Further analysis of gene structure (introns/exons) and conserved motifs showed that they are diverse functions and SAUR-specific domains. The most frequent mechanisms are whole-genome duplication (WGD) and dispersed duplication (DSD), both of which may be important in the growth of the SAUR gene family in Chinese white pear. Moreover, cis-acting elements of the PbrSAUR genes were found in promoter regions associated with the auxin-responsive elements that existed in most of the upstream sequences. Remarkably, the qRT-PCR and transcriptomic data indicated that PbrSAUR13 and PbrSAUR52 were significantly expressed in fruit ripening. Subsequently, subcellular localization experiments revealed that PbrSAUR13 and PbrSAUR52 were localized in the nucleus. Moreover, PbrSAUR13 and PbrSAUR52 were screened for functional verification, and Dangshan pear and frandi strawberry were transiently transformed. Finally, the effects of these two genes on stone cells and lignin were analyzed by phloroglucinol staining, Fourier infrared spectroscopy, and qRT-PCR. It was found that PbrSAUR13 promoted the synthesis and accumulation of stone cells and lignin, PbrSAUR52 inhibited the synthesis and accumulation of stone cells and lignin. In conclusion, these results indicate that PbrSAUR13 and PbrSAUR52 are predominantly responsible for lignin inhibit synthesis, which provides a basic mechanism for further study of PbrSAUR gene functions.

Section: Chromosome Mapping Gene Duplication Events and Ka/ks Ratio A...mentioning

confidence: 99%

Comparative Genomic Analysis of SAUR Gene Family, Cloning and Functional Characterization of Two Genes (PbrSAUR13 and PbrSAUR52) in Pyrus bretschneideri

Manzoor

et al. 2022

IJMS

Proc. Natl. Acad. Sci. U.S.A.

“…S2). Besides ALP genes reported in published studies (13, 23, 24), all other genes were cloned and sequenced ( SI Appendix , Table S1). Alignment of the translated amino acid sequences encoded by the 15 full-length TaALP genes showed that ALPs vary in length from 150 to 285 amino acids ( SI Appendix , Fig.…”

Section: Resultsmentioning

confidence: 99%

New insights into the evolution of wheat avenin-like proteins in wild emmer wheat ( Triticum dicoccoides )

Zhang

Islam

et al. 2018

SignificanceWheat grain avenin-like proteins (ALPs) have functions for dough quality and antifungal activities. A genome-wide characterization of ALP encoding genes in bread wheat is conducted. Results showed that most ALPs are transcriptionally active in developing grains and are up-regulated upon Bgt infection. The allelic diversity of ALPs in 21 natural populations of wild emmer wheat (WEW) in Israel were studied. Many ALP allelic variations in WEW were associated with regional environmental adaption. Our findings demonstrate that the diversifying natural selection through climatic and edaphic factors was a major driving force for the allelic diversity of ALP genes. The results indicate that WEW harbors a high genetic diversity of ALPs utilizable for wheat improvement.

“…Based on the study by Altenbach et al [55], the farinins (ALPs) comprised from 2.6 to 3.1% of the protein in the SDS-extractable polymeric proteins (EPP) and 1.9-2.4% of the protein in the SDS-unextractable polymeric proteins (UPP), and they were influenced by post-anthesis fertilizer. Both type b subunits (bx and by) of ALPs were reported to have non-functional pseudogenes in Brachypodium distachyon L accessions, Triticum dicoccoides, and T. aestivum [47,56]. Most recently, more novel alleles of ALP were found in Aegilops tauschii Coss.…”

Section: Introductionmentioning

confidence: 99%

Characterising avenin-like proteins (ALPs) from albumin/globulin fraction of wheat grains by RP-HPLC, SDS-PAGE, and MS/MS peptides sequencing

Zhang

Juhász

et al. 2020

BMC Plant Biol

Background: Wheat grain avenin-like proteins (ALPs) belong to a recently discovered class of wheat grain storage protein. ALPs in wheat grains not only have beneficial effects on dough quality but also display antifungal activities, which is a novel observation for wheat storage proteins. Previous studies have shown that ALPs are likely present in the albumin/globulin fractions of total protein extract from wheat flour. However, the accumulation characteristics of these ALPs in the mature wheat grain remains unknown. Results: In the present study, a total of 13 ALPs homologs were isolated and characterized in the albumin/globulin fractions of the wheat protein extract. A combination of multiple techniques including RP-HPLC, SDS-PAGE, MALDI-TOF and peptide sequencing were used for accurate separation and identification of individual ALP homolog. The C-terminal TaALP-by-4AL/7DS, TaALP-by-4AL/7AS/7DS, TaALP-bx/4AL/7AS/7DS, TaALP-ay-7DS, TaALP-ay-4AL, TaALPax-4AL, TaALP-ax-7AS, and TaALP-ax-7DS, were separated as individual protein bands from wheat flour for the first time. These unique ALPs peptides were mapped to the latest wheat genome assembly in the IWGSC database. The characteristic defence related proteins present in albumin and globulin fractions, such as protein disulfide-isomerase (PDI), grain softness protein (GSP), alpha-amylase inhibitors (AAIs) and endogenous alpha-amylase/subtilisin inhibitor were also found to co-segregate with these identified ALPs, avenin-3 and α-gliadins. The molecular weight range and the electrophoresis segregation properties of ALPs were characterised in comparison with the proteins containing the tryp_alpha_amyl domain (PF00234) and the gliadin domain (PF13016), which play a role in plant immunity and grain quality. We examined the phylogenetic relationships of the AAIs, GSP, avenin-3, α-gliadins and ALPs, based on the alignment of their functional domains. MALDI-TOF profiling indicated the occurrence of certain post-translations modifications (PTMs) in some ALP subunits. Conclusions: We reported for the first time the complete profiling of ALPs present in the albumin/globulin fractions of wheat grain protein extracts. We concluded that majority of the ALPs homologs are expressed in wheat grains. We found clear evidence of PTMs in several ALPs peptides. The identification of both gliadin domain (PF13016) and Tryp_alpha_amyl domain (PF00234) in the mature forms of ALPs highlighted the multiple functional properties of ALPs in grain quality and disease resistance.