Characterization of a sunflower seed albumin which associates with oil bodies

Thoyts, P. J. E.; Napier, Johnathan A.; Millichip, Mark; Stobart, A. K.; Griffiths, W. T.; Tatham, Arthur S.; Shewry, Peter R.

doi:10.1016/0168-9452(96)04429-9

Cited by 17 publications

(12 citation statements)

References 17 publications

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“…However, subsequent analysis by immunogold EM showed that the protein was present in vivo in protein bodies, and that association with the oil body only occurred in disrupted or lysed tissue [26]. We have observed a similar phenomenon in preparations of sunflower oil bodies, where a previously unidentified class of 2S albumin was found to be tightly associated with the oil bodies after cell lysis, but was present in the protein bodies in vivo [57]. The association between the 2S albumin and the oil body was resistant to repeated washes in high salt buffers, but was disrupted by washing the oil bodies in 9 M urea.…”

Section: Other Proteins Associated With Oil Bodiessupporting

confidence: 50%

The structure and biogenesis of plant oil bodies: the role of the ER membrane and the oleosin class of proteins

1996

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Section: Other Proteins Associated With Oil Bodiessupporting

confidence: 50%

The structure and biogenesis of plant oil bodies: the role of the ER membrane and the oleosin class of proteins

1996

Self Cite

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“…Even within sunflower, there are highly variable albumin genes such as Ha-G5 (Allen et al, 1987), HaBA1 (GenBank AJ275962), pHAO (Thoyts et al, 1996), and SFA8 (Kortt et al, 1991). Our own attempts to find rapidly evolving and constrained sites in PawS1 were hampered by the high observed frequency of insertions and deletions.…”

Section: Discussionmentioning

confidence: 99%

“…These albumins typically vary greatly between species with the main conserved features being an ER targeting signal sequence, richness in Gln, and eight conserved Cys residues (Shewry, 1999). Sunflower contains at least six highly variable albumin-coding genes Ha-G5 (Allen et al, 1987), Ha-BA1, SUNFLOWER ALBUMIN8 (SFA8) (Kortt et al, 1991), and pHAO (Thoyts et al, 1996), along with PawS1 and PawS2 (Mylne et al, 2011). Genetic redundancy provided by large multigene families permits rapid evolution, an example being the great number of highly variable peptides found within venoms of predatory animals (Puillandre et al, 2010;Rokyta et al, 2011), but for the unique PawS1 gene structure, we saw very little or no genetic redundancy.…”

Section: Within Paws1 Genes Both the Pdp And Albumin Regions Are Evomentioning

confidence: 99%

Evolutionary Origins of a Bioactive Peptide Buried within Preproalbumin

et al. 2014

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The de novo evolution of proteins is now considered a frequented route for biological innovation, but the genetic and biochemical processes that lead to each newly created protein are often poorly documented. The common sunflower (Helianthus annuus) contains the unusual gene PawS1 (Preproalbumin with SFTI-1) that encodes a precursor for seed storage albumin; however, in a region usually discarded during albumin maturation, its sequence is matured into SFTI-1, a protease-inhibiting cyclic peptide with a motif homologous to unrelated inhibitors from legumes, cereals, and frogs. To understand how PawS1 acquired this additional peptide with novel biochemical functionality, we cloned PawS1 genes and showed that this dual destiny is over 18 million years old. This new family of mostly backbone-cyclic peptides is structurally diverse, but the protease-inhibitory motif was restricted to peptides from sunflower and close relatives from its subtribe. We describe a widely distributed, potential evolutionary intermediate PawS-Like1 (PawL1), which is matured into storage albumin, but makes no stable peptide despite possessing residues essential for processing and cyclization from within PawS1. Using sequences we cloned, we retrodict the likely stepwise creation of PawS1's additional destiny within a simple albumin precursor. We propose that relaxed selection enabled SFTI-1 to evolve its inhibitor function by converging upon a successful sequence and structure.

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“…Within a single plant species there can be considerable variation in sequence among albumins. The common sunflower possesses six known albumin genes HaG5 (Allen et al 1987), HaB1B2 (GenBank AJ275962), pHAO (Thoyts et al 1996), SFA8 (Kortt et al 1991), PawS1 and PawS2 (Mylne et al 2011). HaG5 and HaB1B2 have a general structure shown Fig.…”

Section: Evolution Of Albuminsmentioning

confidence: 99%

Seed storage albumins: biosynthesis, trafficking and structures

Mylne¹,

Hara‐Nishimura²,

Rosengren³

2014

Functional Plant Biol.

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Abstract. Seed storage albumins are water-soluble and highly abundant proteins that are broken-down during seed germination to provide nitrogen and sulfur for the developing seedling. During seed maturation these proteins are subject to post-translational modifications and trafficking before they are deposited in great quantity and with great stability in dedicated vacuoles. This review will cover the subcellular movement, biochemical processing and mature structures of seed storage napins.Additional keywords: asparaginyl endo-peptidase, napin, seed storage protein, vacuolar processing enzyme, 2S albumin.

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Characterization of a sunflower seed albumin which associates with oil bodies

Cited by 17 publications

References 17 publications

The structure and biogenesis of plant oil bodies: the role of the ER membrane and the oleosin class of proteins

The structure and biogenesis of plant oil bodies: the role of the ER membrane and the oleosin class of proteins

Evolutionary Origins of a Bioactive Peptide Buried within Preproalbumin

Seed storage albumins: biosynthesis, trafficking and structures

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