Structural disorder in proteins brings order to crystal growth in biomineralization

L. Kalmár, Daniel Homola, G. Varga, Peter Tompa

Research output: Contribution to journalArticle

59 Citations (Scopus)

Abstract

Biomineralization, the generation of hard tissues of living organisms, is a process strictly regulated by hormones, enzymes and a range of regulatory proteins of which several resisted structural characterization thus far. Without actual generalizations, there have been scattered observations in the literature for the structural disorder of these proteins. To address this issue in general, we have collected SwissProt proteins involved in the formation of bone and teeth in vertebrates, annotated for biomineralization. All these proteins show an extremely high level of predicted disorder (with a mean of 53%), making them the most disordered functional class of the protein world. Exactly the same feature was established for evolutionarily more distant proteins involved in the formation of the silica wall of marine diatoms and the shell of oysters and other mollusks. Because these proteins also show an extremely biased amino acid composition, such as high negative charge, high frequency of Ser and Asp or Pro residues and repetitiveness, we also carried out a database search with these sequence features for further proteins. This search uncovered several further disordered proteins with clearly related functions, although their annotations made no mention of biomineralization. This general and very strong correlation between biomineralization, structural disorder of proteins and particular sequence features indicates that regulated growth of mineral phase in biology can only be achieved by the assistance of highly disordered proteins.

Original languageEnglish
Pages (from-to)528-534
Number of pages7
JournalBone
Volume51
Issue number3
DOIs
Publication statusPublished - Sep 2012

Fingerprint

Crystallization
Proteins
Diatoms
Ostreidae
Protein Databases
Mollusca
Osteogenesis
Silicon Dioxide
Minerals
Vertebrates
Tooth
Databases
Hormones
Amino Acids

Keywords

  • Bioinformatics
  • Biomineral formation
  • Compositional bias
  • Intrinsically disordered protein
  • Moonlighting

ASJC Scopus subject areas

  • Physiology
  • Endocrinology, Diabetes and Metabolism
  • Histology

Cite this

Structural disorder in proteins brings order to crystal growth in biomineralization. / Kalmár, L.; Homola, Daniel; Varga, G.; Tompa, Peter.

In: Bone, Vol. 51, No. 3, 09.2012, p. 528-534.

Research output: Contribution to journalArticle

Kalmár, L. ; Homola, Daniel ; Varga, G. ; Tompa, Peter. / Structural disorder in proteins brings order to crystal growth in biomineralization. In: Bone. 2012 ; Vol. 51, No. 3. pp. 528-534.
@article{5a173a9242b646edbb3b961cc3fef881,
title = "Structural disorder in proteins brings order to crystal growth in biomineralization",
abstract = "Biomineralization, the generation of hard tissues of living organisms, is a process strictly regulated by hormones, enzymes and a range of regulatory proteins of which several resisted structural characterization thus far. Without actual generalizations, there have been scattered observations in the literature for the structural disorder of these proteins. To address this issue in general, we have collected SwissProt proteins involved in the formation of bone and teeth in vertebrates, annotated for biomineralization. All these proteins show an extremely high level of predicted disorder (with a mean of 53{\%}), making them the most disordered functional class of the protein world. Exactly the same feature was established for evolutionarily more distant proteins involved in the formation of the silica wall of marine diatoms and the shell of oysters and other mollusks. Because these proteins also show an extremely biased amino acid composition, such as high negative charge, high frequency of Ser and Asp or Pro residues and repetitiveness, we also carried out a database search with these sequence features for further proteins. This search uncovered several further disordered proteins with clearly related functions, although their annotations made no mention of biomineralization. This general and very strong correlation between biomineralization, structural disorder of proteins and particular sequence features indicates that regulated growth of mineral phase in biology can only be achieved by the assistance of highly disordered proteins.",
keywords = "Bioinformatics, Biomineral formation, Compositional bias, Intrinsically disordered protein, Moonlighting",
author = "L. Kalm{\'a}r and Daniel Homola and G. Varga and Peter Tompa",
year = "2012",
month = "9",
doi = "10.1016/j.bone.2012.05.009",
language = "English",
volume = "51",
pages = "528--534",
journal = "Bone",
issn = "8756-3282",
publisher = "Elsevier Inc.",
number = "3",

}

TY - JOUR

T1 - Structural disorder in proteins brings order to crystal growth in biomineralization

AU - Kalmár, L.

AU - Homola, Daniel

AU - Varga, G.

AU - Tompa, Peter

PY - 2012/9

Y1 - 2012/9

N2 - Biomineralization, the generation of hard tissues of living organisms, is a process strictly regulated by hormones, enzymes and a range of regulatory proteins of which several resisted structural characterization thus far. Without actual generalizations, there have been scattered observations in the literature for the structural disorder of these proteins. To address this issue in general, we have collected SwissProt proteins involved in the formation of bone and teeth in vertebrates, annotated for biomineralization. All these proteins show an extremely high level of predicted disorder (with a mean of 53%), making them the most disordered functional class of the protein world. Exactly the same feature was established for evolutionarily more distant proteins involved in the formation of the silica wall of marine diatoms and the shell of oysters and other mollusks. Because these proteins also show an extremely biased amino acid composition, such as high negative charge, high frequency of Ser and Asp or Pro residues and repetitiveness, we also carried out a database search with these sequence features for further proteins. This search uncovered several further disordered proteins with clearly related functions, although their annotations made no mention of biomineralization. This general and very strong correlation between biomineralization, structural disorder of proteins and particular sequence features indicates that regulated growth of mineral phase in biology can only be achieved by the assistance of highly disordered proteins.

AB - Biomineralization, the generation of hard tissues of living organisms, is a process strictly regulated by hormones, enzymes and a range of regulatory proteins of which several resisted structural characterization thus far. Without actual generalizations, there have been scattered observations in the literature for the structural disorder of these proteins. To address this issue in general, we have collected SwissProt proteins involved in the formation of bone and teeth in vertebrates, annotated for biomineralization. All these proteins show an extremely high level of predicted disorder (with a mean of 53%), making them the most disordered functional class of the protein world. Exactly the same feature was established for evolutionarily more distant proteins involved in the formation of the silica wall of marine diatoms and the shell of oysters and other mollusks. Because these proteins also show an extremely biased amino acid composition, such as high negative charge, high frequency of Ser and Asp or Pro residues and repetitiveness, we also carried out a database search with these sequence features for further proteins. This search uncovered several further disordered proteins with clearly related functions, although their annotations made no mention of biomineralization. This general and very strong correlation between biomineralization, structural disorder of proteins and particular sequence features indicates that regulated growth of mineral phase in biology can only be achieved by the assistance of highly disordered proteins.

KW - Bioinformatics

KW - Biomineral formation

KW - Compositional bias

KW - Intrinsically disordered protein

KW - Moonlighting

UR - http://www.scopus.com/inward/record.url?scp=84864762380&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84864762380&partnerID=8YFLogxK

U2 - 10.1016/j.bone.2012.05.009

DO - 10.1016/j.bone.2012.05.009

M3 - Article

VL - 51

SP - 528

EP - 534

JO - Bone

JF - Bone

SN - 8756-3282

IS - 3

ER -