Purification and translation of zein messenger RNA from maize endosperm protein bodies

Journal Article · Wed Feb 01 04:00:00 EST 1978 · Proc. Natl. Acad. Sci. U.S.A.; (United States)

DOI:https://doi.org/10.1073/pnas.75.2.696· OSTI ID:6678710

Burr, B; Burr, F A; Rubenstein, I; Simon, M N

The messenger RNAs coding for the zein storage protein have been purified from other contaminating RNAs. The average molecular lengths are 1.1 to 1.2 kilobases, as determined by polyacrylamide gel electrophoresis and by electron microscopy. Products of messenger-dependent protein synthesis in vitro appear to be 1100 and 2000 daltons heavier than the native polypeptides. Zein is like secretory proteins in having a precursor with an additional amino-terminal sequence. Although only one mRNA is seen in polyacrylamide gel electrophoresis, the combined size of the polypeptide products formed exceeds the coding capacity for one message of the size determined in this study. This suggests that there are at least two mRNAs of similar sizes for the zein polypeptides rather than one dicistronic message.

• Research Organization: Brookhaven National Lab., Upton, NY
• OSTI ID: 6678710
• Journal Information: Proc. Natl. Acad. Sci. U.S.A.; (United States), Journal Name: Proc. Natl. Acad. Sci. U.S.A.; (United States) Vol. 75:2; ISSN PNASA
• Country of Publication: United States
• Language: English

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59 BASIC BIOLOGICAL SCIENCES
BIOCHEMISTRY
BIOLOGY
BIOMASS
CEREALS
CHEMISTRY
ELECTRON MICROSCOPY
ELECTROPHORESIS
ENERGY SOURCES
GENETICS
GRAMINEAE
GRASS
LABELLED COMPOUNDS
MAIZE
MESSENGER-RNA
MICROSCOPY
MOLECULAR BIOLOGY
MOLECULAR STRUCTURE
NUCLEIC ACIDS
ORGANIC COMPOUNDS
PLANTS
PROTEINS
PURIFICATION
RENEWABLE ENERGY SOURCES
RNA
SYNTHESIS