Gene cloning and characterization of a soybean (Glycine max L.) LEA protein, GmPM16

Gene cloning and characterization of a soybean (Glycine max L.) LEA protein, GmPM16 Late embryogenesis abundant (LEA) proteins, present in abundance in seeds during the late stages of development, are associated with desiccation tolerance. In the present work, we characterize a soybean LEA protein, GmPM16, with low molecular weight, high pI value, and an unusual amino acid residue distribution along the protein. The transcripts were detected in cotyledon mesophyll cells but not in the vascular system of mature or pod-dried soybean seeds. Circular dichroism (CD) analysis and Fourier transfer infrared (FTIR) spectroscopy indicated that the GmPM16 protein in solution was highly unordered, possessing only partial α-helical structures. However, the protein in sodium dodecyl sulfate (SDS) or trifluoroethanol (TFE) solution or in a dry state exhibited a conformation of abundant α-helical structures. As well, the GmPM16 protein interacts with sugar and forms tightly glassy matrixes in the dry state. The protein may play a role in reducing cellular damage in drying seeds by changing the protein conformation and forming tight cellular glasses. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Molecular Biology Springer Journals

Gene cloning and characterization of a soybean (Glycine max L.) LEA protein, GmPM16

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Publisher
Kluwer Academic Publishers
Copyright
Copyright © 2005 by Springer
Subject
Life Sciences; Biochemistry, general; Plant Sciences; Plant Pathology
ISSN
0167-4412
eISSN
1573-5028
D.O.I.
10.1007/s11103-004-4680-3
Publisher site
See Article on Publisher Site

Abstract

Late embryogenesis abundant (LEA) proteins, present in abundance in seeds during the late stages of development, are associated with desiccation tolerance. In the present work, we characterize a soybean LEA protein, GmPM16, with low molecular weight, high pI value, and an unusual amino acid residue distribution along the protein. The transcripts were detected in cotyledon mesophyll cells but not in the vascular system of mature or pod-dried soybean seeds. Circular dichroism (CD) analysis and Fourier transfer infrared (FTIR) spectroscopy indicated that the GmPM16 protein in solution was highly unordered, possessing only partial α-helical structures. However, the protein in sodium dodecyl sulfate (SDS) or trifluoroethanol (TFE) solution or in a dry state exhibited a conformation of abundant α-helical structures. As well, the GmPM16 protein interacts with sugar and forms tightly glassy matrixes in the dry state. The protein may play a role in reducing cellular damage in drying seeds by changing the protein conformation and forming tight cellular glasses.

Journal

Plant Molecular BiologySpringer Journals

Published: Mar 24, 2005

References

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