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

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 75 ·No. 2 ·1978-02-00 ·Pages 696-700

Burr B, Burr FA, Rubenstein I, Simon MN

Abstract

The messenger RNAs coding for the zein storage protein have been purified from other contaminating RNAs. The average molecular lengths are 1.1-1.2 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.

Authors & Affiliations

4 authors, click to expand affiliations / ORCID

Burr B

Biology Department, Brookhaven National Laboratory, Upton, New York 11973.

Burr F A

Rubenstein I

Simon M N

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Article Info

Journal

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

Abbr.

Proc Natl Acad Sci U S A

ISSN

0027-8424

DOI

10.1073/pnas.75.2.696

Published

1978-02-00

Pages

696-700

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC411323

External Links

PubMed source DOI: 10.1073/pnas.75.2.696 PMC Full Text View journal details

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

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