Unknown,Transcriptomics,Genomics,Proteomics

Dataset Information

Next Generation Sequencing Facilitates Quantitative Analysis of Transcriptomes for Wild Type and Mutants including opaque2, PbfRNAi and PbfRNAi;o2 in Zea mays

ABSTRACT: The goals of this study are to study the regulatory network of the two maize endosperm-specific transcription factors O2 and PBF by 16-DAP endosperm transcriptome profiling (RNA-seq) of their mutants and wild type. The results utilize the expression pattern of global genes regulated by PBF and O2 to elucidate their control for storage compounds synthesis in maize kernels. The 16-DAP endosperm transcriptome of wild type (WT) and mutants including opaque2, PbfRNAi and PbfRNAi;o2 were generated by RNA-seq with three biological replicates per genotype on Illumina HiSeqTM2500.

ORGANISM(S): Zea mays

SUBMITTER: Yongrui Wu

PROVIDER: E-GEOD-79513 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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Publications

Maize endosperm-specific transcription factors O2 and PBF network the regulation of protein and starch synthesis.

Zhang Zhiyong Z Zheng Xixi X Yang Jun J Messing Joachim J Wu Yongrui Y

Proceedings of the National Academy of Sciences of the United States of America 20160912 39

The maize endosperm-specific transcription factors opaque2 (O2) and prolamine-box binding factor (PBF) regulate storage protein zein genes. We show that they also control starch synthesis. The starch content in the PbfRNAi and o2 mutants was reduced by ∼5% and 11%, respectively, compared with normal genotypes. In the double-mutant PbfRNAi;o2, starch was decreased by 25%. Transcriptome analysis reveals that >1,000 genes were affected in each of the two mutants and in the double mutant; these gene ...[more]

PMID: 27621432

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Dataset Information

Next Generation Sequencing Facilitates Quantitative Analysis of Transcriptomes for Wild Type and Mutants including opaque2, PbfRNAi and PbfRNAi;o2 in Zea mays

Publications

Maize endosperm-specific transcription factors O2 and PBF network the regulation of protein and starch synthesis.

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