Glycosylated Polyproline II Rods with Kinks as a Structural Motif in Plant Hydroxyproline-Rich Glycoproteins

Ferris, Patrick J.; Woessner, Jeffrey P.; Waffenschmidt, Sabine; Kilz, S.; Drees, Jutta; Goodenough, Ursula

doi:10.1021/bi0023605

Cited by 102 publications

(138 citation statements)

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“…12 Indeed, mfp-1 has $6 mol % diHyp and 18.2 mol % Hyp, which provide strong inductive effects to favor the trans-proline required in the polyproline II helix. 32 The polyproline II helix also occurs in Hyp-rich extensins of the plant cell wall 33 with typical molar ellipticities of À16,100 and 3900 at 197 and 225 nm, respectively. These helices are monomeric and depend on extensive arabinosylation of Hyp residues to further stabilize the polyproline II helices.…”

Section: Discussionmentioning

confidence: 99%

Three intrinsically unstructured mussel adhesive proteins, mfp‐1, mfp‐2, and mfp‐3: Analysis by circular dichroism

Hwang

Waite

2012

Protein Science

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Mussel foot proteins (mfps) mediate fouling by the byssal holdfast and have been extensively investigated as models for versatile polymer-mediated underwater adhesion and coatings. However, insights into the structural properties of mfps have lagged far behind the nanomechanical advances, owing in part to the inability of these proteins to crystallize as well as their limited solubility. Here, solution secondary structures of mfp-1, mfp-2, and mfp-3, localized in the mussel byssal cuticle, adhesive plaque, and plaque-substratum interface, respectively, were investigated using circular dichroism. All three have significant extended coil solution structure, but two, mfp-1 and mfp-2, appear to have punctuated regions of structure separated by unstructured domains. Apart from its punctuated distribution, the structure in mfp-1 resembles other structural proteins such as collagen and plant cell-wall proteins with prominent polyproline II helical structure. As in collagen, PP II structure of mfp-1 is incrementally disrupted by increasing the temperature and by raising pH. However, no recognizable change in mfp-1's PP II structure was evident with the addition with Ca 21 and Fe 31 . In contrast, mfp-2 exhibits Ca 21 -and disulfidestabilized epidermal growth factor-like domains separated by unstructured sequence. Mfp-2 showed calcium-binding ability. Bound calcium in mfp-2 was not removed by chelation at pH 5.5, but it was released upon reduction of disulfide bonds. Mfp-3, in contrast, appears to consist largely of unstructured extended coils.

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Section: Discussionmentioning

confidence: 99%

Three intrinsically unstructured mussel adhesive proteins, mfp‐1, mfp‐2, and mfp‐3: Analysis by circular dichroism

Hwang

Waite

2012

Protein Science

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“…Such protein domains are subject to glycosylation and may form fibrous structures (Woessner and Goodenough, 1992;Ferris et al, 2001Ferris et al, , 2005. The predicted fibrous structures of the three GAS proteins are flanked by domains that were predicted to form globular structures.…”

Section: Discussionmentioning

confidence: 99%

“…We next tested whether GAS28, GAS30, and GAS31 may exhibit similarity to C. reinhardtii cell wall glycoproteins GP1, GP2 Ferris et al, 2001; GP2 GenBank accession no. AY596305), VSP3 (Woessner et al, 1994), class IV cDNA coding for a 34-kD polypeptide (Ferris and Goodenough, 1987;Woessner and Goodenough, 1989), and ZSP-2 (Suzuki et al, 2000).…”

Section: Analysis Of Predicted Gene Productsmentioning

confidence: 99%

“…AY596305), VSP3 (Woessner et al, 1994), class IV cDNA coding for a 34-kD polypeptide (Ferris and Goodenough, 1987;Woessner and Goodenough, 1989), and ZSP-2 (Suzuki et al, 2000). No similarities in the amino acid sequences of the N-terminal or the C-terminal domain were detected, although these proteins are known to be composed of globular domains with Pro-rich stretches Woessner et al, 1994;Ferris et al, 2001). …”

Section: Analysis Of Predicted Gene Productsmentioning

confidence: 99%

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Mating-Induced Shedding of Cell Walls, Removal of Walls from Vegetative Cells, and Osmotic Stress Induce Presumed Cell Wall Genes in Chlamydomonas

Hoffmann

Beck

2005

Plant Physiology

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The first step in sexual differentiation of the unicellular green alga Chlamydomonas reinhardtii is the formation of gametes. Three genes, GAS28, GAS30, and GAS31, encoding Hyp-rich glycoproteins that presumably are cell wall constituents, are expressed in the late phase of gametogenesis. These genes, in addition, are activated by zygote formation and cell wall removal and by the application of osmotic stress. The induction by zygote formation could be traced to cell wall shedding prior to gamete fusion since it was seen in mutants defective in cell fusion. However, it was absent in mutants defective in the initial steps of mating, i.e. in flagellar agglutination and in accumulation of adenosine 3#,5#-cyclic monophosphate in response to this agglutination. Induction of the three GAS genes was also observed when cultures were exposed to hypoosmotic or hyperosmotic stress. To address the question whether the induction seen upon cell wall removal from both gametes and vegetative cells was elicited by osmotic stress, cell wall removal was performed under isosmotic conditions. Also under such conditions an activation of the genes was observed, suggesting that the signaling pathway(s) is (are) activated by wall removal itself.

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“…This structure plays a role in several biochemical processes including signal transduction, transcription, cell motility, and the immune response (Creamer, 1998;Stapley and Creamer, 1999). PII helices are major features of collagens (Pauling and Corey, 1951) and plant cell wall proteins (Ferris et al, 2001). PII structures are also found in the antifreeze glycoproteins of polar fish (Lane et al, 1998(Lane et al, , 2000.…”

Section: Potential Physiological Roles Of Pii Structuresmentioning

confidence: 99%

Conformation of a Group 2 Late Embryogenesis Abundant Protein from Soybean. Evidence of Poly (l-Proline)-type II Structure

et al. 2003

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Late embryogenesis abundant (LEA) proteins are members of a large group of hydrophilic, glycine-rich proteins found in plants, algae, fungi, and bacteria known collectively as hydrophilins that are preferentially expressed in response to dehydration or hyperosmotic stress. Group 2 LEA (dehydrins or responsive to abscisic acid) proteins are postulated to stabilize macromolecules against damage by freezing, dehydration, ionic, or osmotic stress. However, the structural and physicochemical properties of group 2 LEA proteins that account for such functions remain unknown. We have analyzed the structural properties of a recombinant form of a soybean (Glycine max) group 2 LEA (rGmDHN1). Differential scanning calorimetry of purified rGmDHN1 demonstrated that the protein does not display a cooperative unfolding transition upon heating. Ultraviolet absorption and circular dichroism spectroscopy revealed that the protein is in a largely hydrated and unstructured conformation in solution. However, ultraviolet absorption and circular dichroism measurements collected at different temperatures showed that the protein exists in equilibrium between two extended conformational states: unordered and left-handed extended helical or poly (l-proline)-type II structures. It is estimated that 27% of the residues of rGmDHN1 adopt or poly (l-proline)-type II-like helical conformation at 12°C. The content of extended helix gradually decreases to 15% as the temperature is increased to 80°C. Studies of the conformation of the protein in solution in the presence of liposomes, trifluoroethanol, and sodium dodecyl sulfate indicated that rGmDHN1 has a very low intrinsic ability to adopt ␣-helical structure and to interact with phospholipid bilayers through amphipathic ␣-helices. The ability of the protein to remain in a highly extended conformation at low temperatures could constitute the basis of the functional role of GmDHN1 in the prevention of freezing, desiccation, ionic, or osmotic stress-related damage to macromolecular structures. Group 2 LEA proteins or dehydrins or responsive to abscisic acid (RAB) proteins were originally identified as the "D-11" family of LEA proteins in developing cotton (Gossypium hirsutum) embryos (Baker et al., 1988;Dure et al., 1989;Hughes and Galau, 1989). Dehydrins appear to be ubiquitously expressed in gymnosperms (Jarvis et al., 1996;Richard et al., 2000) and angiosperms (Campbell and Close, 1997;Close, 1997). Immunological surveys have also detected dehydrin-related proteins in algae, yeast, and cyanobacteria (Close and Lammers, 1993; Campbell and Close, 1997;Close, 1997;Li et al., 1998;Mtwisha et al., 1998). Group 2 LEA proteins form a subset of evolutionarily conserved Gly-rich, hydrophilic proteins associated with adaptation to hyperosmotic conditions (Garay-Arroyo et al., 2000). Dehydrins are induced typically in maturing seeds or vegetative tissues following salinity, dehydration, cold, or freezing stress or abscisic acid (ABA) treatment (Close, 1996(Close, , 1997 Campbell and Close, 1997). Numero...

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Glycosylated Polyproline II Rods with Kinks as a Structural Motif in Plant Hydroxyproline-Rich Glycoproteins

Cited by 102 publications

References 63 publications

Three intrinsically unstructured mussel adhesive proteins, mfp‐1, mfp‐2, and mfp‐3: Analysis by circular dichroism

Three intrinsically unstructured mussel adhesive proteins, mfp‐1, mfp‐2, and mfp‐3: Analysis by circular dichroism

Mating-Induced Shedding of Cell Walls, Removal of Walls from Vegetative Cells, and Osmotic Stress Induce Presumed Cell Wall Genes in Chlamydomonas

Conformation of a Group 2 Late Embryogenesis Abundant Protein from Soybean. Evidence of Poly (l-Proline)-type II Structure

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