NDLI: Quantification of cellular protein expression and molecular features of group 3 LEA proteins from embryos of Artemia franciscana

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Quantification of cellular protein expression and molecular features of group 3 LEA proteins from embryos of Artemia franciscana

Content Provider	Springer Nature Link
Author	Boswell, Leaf C. Moore, Daniel S. Hand, Steven C.
Copyright Year	2013
Abstract	Late embryogenesis abundant (LEA) proteins are highly hydrophilic, low complexity proteins whose expression has been correlated with desiccation tolerance in anhydrobiotic organisms. Here, we report the identification of three new mitochondrial LEA proteins in anhydrobiotic embryos of Artemia franciscana, AfrLEA3m_47, AfrLEA3m_43, and AfrLEA3m_29. These new isoforms are recognized by antibody raised against recombinant AfrLEA3m, the original mitochondrial-targeted LEA protein previously reported from these embryos; mass spectrometry confirms all four proteins share sequence similarity. The corresponding messenger RNA (mRNA) species for the four proteins are readily amplified from total complementary DNA (cDNA) prepared from embryos. cDNA sequences of the four mRNAs are quite similar, but each has a stretch of sequence that is absent in at least one of the others, plus multiple single base pair differences. We conclude that all four mitochondrial LEA proteins are products of independent genes. Each possesses a mitochondrial targeting sequence, and indeed Western blots performed on extracts of isolated mitochondria clearly detect all four isoforms. Based on mass spectrometry and sodium dodecyl sulfate polyacrylamide gel electrophoresis migration, the cytoplasmic-localized AfrLEA2 exists primarily as a homodimer in A. franciscana. Quantification of protein expression for AfrLEA2, AfrLEA3m, AfrLEA3m_43, and AfrLEA3m_29 as a function of development shows that cellular concentrations are highest in diapause embryos and decrease during development to low levels in desiccation-intolerant nauplius larvae. When adjustment is made for mitochondria matrix volume, the effective concentrations of cytoplasmic versus mitochondrial group 3 LEA proteins are similar in vivo, and the values provide guidance for the design of in vitro functional studies with these proteins.
Starting Page	329
Ending Page	341
Page Count	13
File Format	PDF
ISSN	13558145
Journal	Cell Stress and Chaperones
Volume Number	19
Issue Number	3
e-ISSN	14661268
Language	English
Publisher	Springer Netherlands
Publisher Date	2013-09-06
Publisher Place	Dordrecht
Access Restriction	Subscribed
Subject Keyword	Intrinsically disordered proteins (IDPs) Mitochondrion Desiccation tolerance Brine shrimp Biomedicine general Cell Biology Biochemistry Immunology Cancer Research Neurosciences
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry

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Quantification of cellular protein expression and molecular features of group 3 LEA proteins from embryos of Artemia franciscana.

Group 1 LEA proteins contribute to the desiccation and freeze tolerance of Artemia franciscana embryos during diapause

Group 1 LEA proteins contribute to the desiccation and freeze tolerance of Artemia franciscana embryos during diapause.

Quantification of cellular protein expression and molecular features of group 3 LEA proteins from embryos of Artemia franciscana

Group 1 LEA proteins contribute to the desiccation and freeze tolerance of Artemia franciscana embryos during diapause

Molecular approaches for improving desiccation tolerance: insights from the brine shrimp Artemia franciscana

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Cyst viability and stress tolerance upon heat shock protein 70 knockdown in the brine shrimp Artemia franciscana.

Quantification of cellular protein expression and molecular features of group 3 LEA proteins from embryos of Artemia franciscana

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Quantification of cellular protein expression and molecular features of group 3 LEA proteins from embryos of Artemia franciscana