Proteomic profiling of maize opaque endosperm mutants reveals selective accumulation of lysine-enriched proteins

Abstract

HighlightProteome-wide assessment across an isogenic collection of cloned opaque endosperm mutants caused by different and well-characterized mutations provided biological insight into proteome rebalancing and favorable amino acid compositional changes.

Shotgun proteomics of the barley seed proteome

“…Recently, deep proteome analysis of the gerantoplasts from the inner integuments of the developing seeds of Jatropha curcas using an in-solution digestion followed by LC MS/MS identified 812 proteins [22]. A comparison of the seed proteomes of the various opaque mutants of maize identified nearly 2700 proteins using the LC MS/MS strategy [16]. Thus the number of proteins identified in the current study is comparable to other deep proteome studies in the recently published literature.…”

“…One of the recent trends in shotgun proteomics is the use of label-free methods for protein quantitation [11]. A number of reports on the use of gel-free label-free quantitative proteomics have been conducted in plants including Arabidopsis [12], tomato [13], soybeans [14], barley [15] and corn [16]. …”

Editing of an Alpha-Kafirin Gene Family Increases, Digestibility and Protein Quality in Sorghum

“…The regulatory mechanisms that result in increases in some seed proteins when others are reduced are unknown. However, increases in nonprolamins occur both at the global level (Hunter et al, 2002) and at the level of individual Lys-enriched proteins (Morton et al, 2016).…”

Comprehensive proteomic analysis of developing protein bodies in maize (Zea mays) endosperm provides novel insights into its biogenesis

“…The remaining proteins were related to other biological categories, including development and growth, regulation, signal transduction, and cellular component organization. Similarly, the biological processes enriched in a recently reported maize non-zein proteome included protein transport, protein folding, proteolysis, and biosynthetic processes (Morton et al , 2016). Noticeably, this non-zein proteome was derived from the whole kernels whereas our PB proteome is restricted to proteins tightly adhered to or resided in PBs.…”