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  Soybean ENOD40 encodes two peptides that bind to sucrose synthase

Röhrig, H., Schmidt, J., Miklashevichs, E., Schell, J., & John, M. (2002). Soybean ENOD40 encodes two peptides that bind to sucrose synthase. Proceedings of the National Academy of Sciences of the United States of America, 99(4), 1915-1920.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-3E0E-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-3E0F-B
Genre: Journal Article

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 Creators:
Röhrig, H.1, Author              
Schmidt, J.1, 2, Author              
Miklashevichs, E., Author
Schell, J.1, Author              
John, M.1, Author              
Affiliations:
1Dept. of Genetic Principles of Plant Breeding (Jozef Schell), MPI for Plant Breeding Research, Max Planck Society, ou_1113567              
2Mass Spectrometry, MPI for Plant Breeding Research, Max Planck Society, ou_1113575              

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Free keywords: translation; short open reading frames; peptide signals
 Abstract: ENOD40 is expressed at an early stage in root nodule organogenesis in legumes. Identification of ENOD40 homologs in nonleguminous plants suggests that this gene may have a more general biological function. In vitro translation of soybean ENOD40 mRNA in wheat germ extracts revealed that the conserved nucleotide sequence at the 5' end (region 1) encodes two peptides of 12 and 24 aa residues (peptides A and B). These peptides are synthesized de novo from very short, overlapping ORFs. Appropriate ORFs are present in all legume ENOD40s studied thus far. In this case small peptides are directly translated from polycistronic eukaryotic mRNA. The 24-aa peptide B was detected in nodules by Western blotting. Both peptides specifically bind to the same 93-kDa protein, which was affinity purified from soybean nodules. Using pepticle mass fingerprinting, we identified this binding protein as nodulin 100, which is a subunit of sucrose synthase. Based on our data we suggest that ENOD40 peptides are involved in the control of sucrose use in nitrogen-fixing nodules.

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Language(s): eng - English
 Dates: 2002-02-19
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: eDoc: 42411
ISI: 000174031100032
 Degree: -

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Title: Proceedings of the National Academy of Sciences of the United States of America
  Alternative Title : Proc. Natl. Acad. Sci. U. S. A.
Source Genre: Journal
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Publ. Info: -
Pages: - Volume / Issue: 99 (4) Sequence Number: - Start / End Page: 1915 - 1920 Identifier: ISSN: 0027-8424