Structural analysis of a repetitive protein sequence motif in strepsirrhine primate amelogenin

Rodrigo Lacruz, Rajamani Lakshminarayanan, Keith M. Bromley, Joseph G. Hacia, Timothy Bromage, Malcolm L. Snead, Janet Moradian-Oldak, Michael L. Paine

Research output: Contribution to journalArticle

Abstract

Strepsirrhines are members of a primate suborder that has a distinctive set of features associated with the development of the dentition. Amelogenin (AMEL), the better known of the enamel matrix proteins, forms 90% of the secreted organic matrix during amelogenesis. Although AMEL has been sequenced in numerous mammalian lineages, the only reported strepsirrhine AMEL sequences are those of the ring-tailed lemur and galago, which contain a set of additional proline-rich tandem repeats absent in all other primates species analyzed to date, but present in some non-primate mammals. Here, we first determined that these repeats are present in AMEL from three additional lemur species and thus are likely to be widespread throughout this group. To evaluate the functional relevance of these repeats in strepsirrhines, we engineered a mutated murine amelogenin sequence containing a similar proline-rich sequence to that of Lemur catta. In the monomeric form, the MQP insertions had no influence on the secondary structure or refolding properties, whereas in the assembled form, the insertions increased the hydrodynamic radii. We speculate that increased AMEL nanosphere size may influence enamel formation in strepsirrhine primates.

Original languageEnglish (US)
Article numbere18028
JournalPLoS One
Volume6
Issue number3
DOIs
StatePublished - 2011

Fingerprint

Amelogenin
Amino Acid Motifs
Nucleic Acid Repetitive Sequences
Structural analysis
Primates
amino acid sequences
enamel
Lemur
proline
nanospheres
Galago
Proteins
tandem repeat sequences
Proline
hydrodynamics
teeth
Amelogenesis
mammals
Nanospheres
Tandem Repeat Sequences

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Medicine(all)

Cite this

Lacruz, R., Lakshminarayanan, R., Bromley, K. M., Hacia, J. G., Bromage, T., Snead, M. L., ... Paine, M. L. (2011). Structural analysis of a repetitive protein sequence motif in strepsirrhine primate amelogenin. PLoS One, 6(3), [e18028]. https://doi.org/10.1371/journal.pone.0018028

Structural analysis of a repetitive protein sequence motif in strepsirrhine primate amelogenin. / Lacruz, Rodrigo; Lakshminarayanan, Rajamani; Bromley, Keith M.; Hacia, Joseph G.; Bromage, Timothy; Snead, Malcolm L.; Moradian-Oldak, Janet; Paine, Michael L.

In: PLoS One, Vol. 6, No. 3, e18028, 2011.

Research output: Contribution to journalArticle

Lacruz, R, Lakshminarayanan, R, Bromley, KM, Hacia, JG, Bromage, T, Snead, ML, Moradian-Oldak, J & Paine, ML 2011, 'Structural analysis of a repetitive protein sequence motif in strepsirrhine primate amelogenin', PLoS One, vol. 6, no. 3, e18028. https://doi.org/10.1371/journal.pone.0018028
Lacruz, Rodrigo ; Lakshminarayanan, Rajamani ; Bromley, Keith M. ; Hacia, Joseph G. ; Bromage, Timothy ; Snead, Malcolm L. ; Moradian-Oldak, Janet ; Paine, Michael L. / Structural analysis of a repetitive protein sequence motif in strepsirrhine primate amelogenin. In: PLoS One. 2011 ; Vol. 6, No. 3.
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