Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0018028
Title: Structural analysis of a repetitive protein sequence motif in strepsirrhine primate amelogenin
Authors: Lacruz R.S.
Lakshminarayanan R. 
Bromley K.M.
Hacia J.G.
Bromage T.G.
Snead M.L.
Moradian-Oldak J.
Paine M.L.
Keywords: amelogenin
chimeric protein
glutamine
methionine
proline
amelogenin
recombinant protein
amino acid sequence
article
circular dichroism
controlled study
female
gene insertion
human
hydrodynamics
male
mouse
nonhuman
nucleotide repeat
nucleotide sequence
prosimian
protein assembly
protein engineering
protein motif
protein secondary structure
sequence analysis
tooth development
amino acid sequence
animal
chemistry
exon
genetics
kinetics
light
metabolism
molecular cloning
molecular genetics
pH
primate
protein refolding
protein unfolding
radiation scattering
sequence alignment
temperature
Galago
Lemur
Lemur catta
Mammalia
Murinae
Primates
Amelogenin
Amino Acid Motifs
Amino Acid Sequence
Animals
Circular Dichroism
Cloning, Molecular
Exons
Humans
Hydrogen-Ion Concentration
Kinetics
Light
Mice
Molecular Sequence Data
Primates
Protein Refolding
Protein Unfolding
Recombinant Proteins
Repetitive Sequences, Amino Acid
Scattering, Radiation
Sequence Alignment
Temperature
Issue Date: 2011
Citation: Lacruz R.S., Lakshminarayanan R., Bromley K.M., Hacia J.G., Bromage T.G., Snead M.L., Moradian-Oldak J., Paine M.L. (2011). Structural analysis of a repetitive protein sequence motif in strepsirrhine primate amelogenin. PLoS ONE 6 (3) : e18028. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0018028
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. © 2011 Lacruz et al.
Source Title: PLoS ONE
URI: https://scholarbank.nus.edu.sg/handle/10635/162054
ISSN: 19326203
DOI: 10.1371/journal.pone.0018028
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