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Accumulation of foreign polypeptides to rice seed protein body type I using prolamin portion sequences

Overview of attention for article published in Plant Cell Reports, December 2016
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Title
Accumulation of foreign polypeptides to rice seed protein body type I using prolamin portion sequences
Published in
Plant Cell Reports, December 2016
DOI 10.1007/s00299-016-2097-5
Pubmed ID
Authors

Ai Sasou, Takanari Shigemitsu, Shigeto Morita, Takehiro Masumura

Abstract

Rice prolamins are accumulated in endoplasmic reticulum (ER)-derived proteins bodies, although conserved sequences retained in ER are not confirmed. We investigated portion sequences of prolamins that must accumulate in PB-Is. Rice seed prolamins are accumulated in endoplasmic reticulum (ER)-derived protein body type I (PB-I), but ER retention sequences in rice prolamin polypeptides have not been confirmed. Here we investigated the lengths of the prolamin portion sequences required for accumulation in PB-Is. Of the rice prolamins, we compared 13a and 13b prolamins because the amino acid sequences of these prolamins are quite similar except for the presence or absence of Cys-residues. We also generated and analyzed transgenic rice expressing several prolamin portion sequence-GFP fusion proteins. We observed that in 13a prolamin, when the portion sequences were extended more than the 68th amino acid residue from the initiating methionine, the prolamin portion sequence-GFP fusion proteins were accumulated in PB-Is. In 13b prolamin, when the portion sequences were extended by more than the 82nd amino acid residue from the initiating methionine, the prolamin portion sequence-GFP fusion proteins were accumulated in PB-Is. When those fusion proteins were extracted under non-reduced or reduced conditions, the 13a prolamin portion sequence-GFP fusion proteins in PB-Is were soluble under only the reduced condition. In contrast, 13b prolamin portion sequence-GFP fusion proteins were soluble under both non-reduced and reduced conditions. These results suggest that the accumulation of 13a prolamin in PB-Is is associated with the formation of disulfide bonds and/or hydrophobicity in 13a prolamin polypeptide, whereas the accumulation of 13b prolamin in PB-Is was less involved in the formation of disulfide bonds.

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Unknown 1 100%

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Readers by professional status Count As %
Student > Doctoral Student 1 100%
Readers by discipline Count As %
Agricultural and Biological Sciences 1 100%

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 19 June 2019.
All research outputs
#11,759,386
of 13,248,851 outputs
Outputs from Plant Cell Reports
#1,373
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Outputs of similar age
#220,252
of 257,333 outputs
Outputs of similar age from Plant Cell Reports
#28
of 35 outputs
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