Sequences of Two Highly Divergent Canine Type c Lysozymes: Implications for the Evolutionary Origins of the Lysozyme/α-Lactalbumin Superfamily

Grobler, Jay A.; Rao, K.R.S. Sambasiva; Pervaiz, Syed; Brew, Keith

doi:10.1006/abbi.1994.1399

Cited by 61 publications

(43 citation statements)

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“…Conversely, acquisition of calcium binding by a non-calcium binding lysozyme might be favoured because the product would be more stable. It has been proposed (Grobler et al, 1994) that calcium-binding activity is an ancient feature of the lysozyme-o~-lactalbumin superfamily which has been lost from the non-calcium-binding gene line; however, this seems improbable if the loss of calcium significantly decreases the stability of these proteins under physiological conditions. In that case it would seem more likely that calcium-binding lysozymes such 360 CALCIUM-BINDING ECHIDNA MILK LYSOZYME …”

Section: Discussionmentioning

confidence: 99%

“…for C a atoms is 1.03 ,~). This is not surprising since the lysozyme sequence which is closest to echidna is pigeon (Grobler et al, 1994), despite their distant evolutionary relationship. In fact PEWL has most of the eccentric characteristics of EML, including the short C-terminal strand terminating in a cysteine residue and the calcium-binding loop, and only lacks the shift in the sequence of the most N-terminal cysteine.…”

Section: Comparison With Other Lysozyme Structuresmentioning

confidence: 95%

“…Since then a number of other naturally occurring c-type lysozymes have been proposed to have a calcium binding site on the basis of their aminoacid sequences. These include the lysozymes of donkey (Godovac-Zimmermann, Conti & Napolitano, 1988), dog, cat and hooded seal, (Grobler, Rao, Pervaiz & Brew, 1994) as well as echidna (Teahan, McKenzie, Shaw & Griffiths, 1991). It is generally assumed that all these lysozymes bind calcium, but so far this has been unequivocally demonstrated only for the equine, pigeon and canine enzymes.…”

Section: Introductionmentioning

confidence: 99%

“…The precise time of the gene duplication event is, however, still disputed. More recent studies, including the discovery of calciumbinding lysozymes and the sequencing of marsupial and monotreme proteins, have provided new evidence for the debate but have not resolved the question of whether the calcium-binding lysozymes are the genuine ancestors of the oMactalbumins (Grobler et al, 1994;Nitta & Sugai, 1989).…”

Section: Introductionmentioning

confidence: 99%

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Structure of the Calcium-Binding Echidna Milk Lysozyme at 1.9 Å Resolution

Guss¹,

Messer²,

Costello³

et al. 1997

Acta Cryst D

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A lysozyme isolated from the milk of a monotreme, the echidna, Tachyglossus aculeatus multiaculeatus, has been crystallized (space group P21, with unit-cell dimensions a = 37.1, b = 42.0, c = 38.1 ~, /3 = 91 ° and Z= 2) and the structure refined to an R value of 0.167 for all measured data in the resolution range 7.0-1.9 ]k. It had previously been inferred from sequence homology with o~-lactalbumins that echidna milk lysozyme (EML) would bind one calcium ion per molecule. This has been confirmed in the present study in which the largest peak in a difference Fourier synthesis is associated with a calcium ion. The calcium binding site of EML is very similar to that observed in baboon and human c~-lactalbumins, and in a human lysozyme engineered to contain a calcium-binding site. The overall fold of the protein is similar to that of chick-type lysozymes. EML, like pigeon lysozyme, has only 125 residues terminating at a cysteine but in EML this forms a disulfide with a cysteine at residue 9 whereas the equivalent cysteine residue in all other lysozymes of known sequence occurs at position 6. These changes cause some minor structural rearrangements. The binding of calcium appears to have had little effect on the polypeptide backbone conformation and caused only small changes in the conformation of side chains coordinating the calcium ion. A homology modelling study [Acharya, Stuart, Phillips, McKenzie & Teahan (1994). J. Protein Chem. 13(6), 569-584] correctly predicted the overall structure of EML and the nature of its calcium binding site but generally failed to model some more subtle differences observed in the EML structure as evidenced by the fact that the homology model more closely resembles the starting structure from which the model was derived than it does the crystal structure.

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Section: Discussionmentioning

confidence: 99%

Section: Comparison With Other Lysozyme Structuresmentioning

confidence: 95%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Structure of the Calcium-Binding Echidna Milk Lysozyme at 1.9 Å Resolution

Guss¹,

Messer²,

Costello³

et al. 1997

Acta Cryst D

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“…It is also suggested that there are other mammalian calciumbinding lysozymes, e.&., from echidna and canine milk (Teahan et al, 1991;Grobler et al, 1994). Echidna is a member of monotreme, egg-laying mammals.…”

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confidence: 99%

Calcium‐binding and structural stability of echidna and canine milk lysozymes

1998

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For echidna and canine milk lysozymes, which were presumed to be the calcium-binding lysozymes by their amino acid sequences, we have quantitated their calcium-binding strength and examined their guanidine unfolding profiles.The calcium-binding constants of echidna and canine lysozymes were determined to be 8.6 X 10' M" and 8.9 X IO6 M" in 0.1 M KC1 at pH 7.1 and 20 "C, respectively. The unfolding of decalcified canine lysozyme proceeds in the same manner as that of a-lactalbumin, through a stable molten globule intermediate. However, neither calcium-bound nor decalcified echidna lysozyme shows a stable molten globule intermediate. This unfolding profile of echidna lysozyme is identical to that of conventional lysozymes and pigeon egg-white lysozyme, avian calcium-binding lysozyme. This result supports the suggestion of Prager and Jolles (Prager EM, Jolles P. 1996. Animal lysozymes c and g: An overview. In: Jolles P, ed. Lysozymes: Model enzymes in biochemistry and biology. Basel-Boston-Berlin: Birkhauzer Verlag. pp 9-3 1) that the lineage of avian and echidna calcium-binding lysozymes and that of eutherian calcium-binding lysozymes diverged separately from that of conventional lysozymes.

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Enhancement of thermal stability and inhibition of protein aggregation by osmolytic effect of hydroxyproline

Kar

Kishore

2007

Biopolymers

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A combination of spectroscopic, calorimetric, and microscopic studies to understand the effect of hydroxyproline on the thermal stability, conformation, biological activity, and aggregation of proteins has been investigated. Significantly increased protein stability and suppression of aggregation is achieved in the presence of hydroxyproline. For example, exceptional increase in the thermal stability of lysozyme up to 26.4 degrees C and myoglobin up to 31.8 degrees C is obtained in the presence of hydroxyproline. The increased thermal stability of the proteins is observed to be accompanied with significant rise of the catalytic activity. Hydroxyproline is observed to prevent lysozyme fibril formation in vitro. Fluorescence and circular dichroism studies indicate induction of tertiary structures of the studied proteins in the presence of hydroxyproline. Preferential hydration of the native state is found to be crucial for the mechanism of protein stabilization by hydroxyproline. We compared the effect of hydroxyproline to that of proline and observed similar increase in the activity and suppression of protein aggregation. The results demonstrate the use of hydroxyproline as a protein stabilizer and in the prevention of protein aggregation and fibril formation.

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Sequences of Two Highly Divergent Canine Type c Lysozymes: Implications for the Evolutionary Origins of the Lysozyme/α-Lactalbumin Superfamily

Cited by 61 publications

References 0 publications

Structure of the Calcium-Binding Echidna Milk Lysozyme at 1.9 Å Resolution

Structure of the Calcium-Binding Echidna Milk Lysozyme at 1.9 Å Resolution

Calcium‐binding and structural stability of echidna and canine milk lysozymes

Enhancement of thermal stability and inhibition of protein aggregation by osmolytic effect of hydroxyproline

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