Abstract
The Roegneria of Triticeae is a large genus including about 130 allopolyploid species. Little is known about its high-molecular-weight glutenin subunits (HMW-GSs). Here, we reported six novel HMW-GS genes from R. nakaii and R. alashanica. Sequencing indicated that Rny1, Rny3, and Ray1 possessed intact open reading frames (ORFs), whereas Rny2, Rny4, and Ray2 harbored in-frame stop codons. All of the six genes possessed a similar primary structure to known HMW-GS, while showing some unique characteristics. Their coding regions were significantly shorter than Glu-1 genes in wheat. The amino acid sequences revealed that all of the six genes were intermediate towards the y-type. The phylogenetic analysis showed that the HMW-GSs from species with St, StY, or StH genome(s) clustered in an independent clade, varying from the typical x- and y-type clusters. Thus, the Glu-1 locus in R. nakaii and R. alashanica is a very primitive glutenin locus across evolution. The six genes were phylogenetically split into two groups clustered to different clades, respectively, each of the two clades included the HMW-GSs from species with St (diploid and tetraploid species), StY, and StH genomes. Hence, it is concluded that the six Roegneria HMW-GS genes are from two St genomes undergoing slight differentiation.
Highlights
High-molecular-weight glutenin subunits (HMW-GSs) are the major seed storage proteins in the endosperm of wheat and its related species
As per the above characteristics, these six Roegneria HMW-GS genes are not a typical y-type gene, and should rather be classed into an intermediate type inclining towards the y-type
The recombinant plasmids were transformed into BL21(DE3)pLysS competent cells, and HMW-GSs were expressed in E. coli by inducing with 1 mM isopropyl β-D-1-thiogalactopyranoside (IPTG) for 6 h
Summary
High-molecular-weight glutenin subunits (HMW-GSs) are the major seed storage proteins in the endosperm of wheat and its related species. HHiitthheerrttoo,, lliittttllee iinnffoorrmmaattiioonn iiss aavvaaiillaabbllee oonn tthhee RRooeeggnneerriiaa HHMMWW--GGSSss aanndd tthheeiirr ccooddiinngg ggeenneess. AA ssttrriikkiinngg ffeeaattuurree ooff tthheessee RRooeeggnneerriiaa HHMMWW--GGSSss wwaass tthheeiirr ccoonnssiiddeerraabbllyy ffaasstteerr eelleeccttrroopphhoorreettiicc wmsmswouureoeobbrrωbbueueii-nnlldgidiiittlittiiiisesea((ttsisidrrnniicicbbnoGoGuusmmTTtteae1p1pdpdaaooprrififneeenRRaddtrt..hhtetnnoeodeaatkstks(hhaaaaFeimeimiiig))sseeuwuwurrbbraeaeeuusgsgn1niffio)aiioa.ttnsssnsIttnefewfwrrrrooahhttmdmhehedraarecnecinitoionintmtomhhnllaomamo,ttwwtooooh-nn-ffmemtrwtwhoheoehlehlewee1ec1caDaeuDuttrl.yl.eyaa1AA1rrs2--2ddowwsmddsueeuiiieibttbggiiuoouhohnnnnttthaiaigtgtlellllloroyuyuff,,tptCeettCrhhnnhoheeiitinniennmmiesesnosuousebebbbbiiSauuSllinpinnpttdyryiirttiisnssnoogwfg(f(LL,,ttihaMhMathneneWWddlslaalt--rtorhGGhggweeeSSessesssseetr))t electrophoretic mobility on SDS-PAGE than those of the HMW-GS homologs which were not recognized by the antibody. We speculated that those protein bands might be gliadin homologs. There were some other protein bands with slower electrophoretic mobility on SDS-PAGE than those of the HMW-GS homologs which were not recognized by the antibody.
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