Conservation of the human integrin-type beta-propeller domain in bacteria.

Integrins are heterodimeric cell-surface receptors with key functions in cell-cell and cell-matrix adhesion. Integrin α and β subunits are present throughout the metazoans, but it is unclear whether the subunits predate the origin of multicellular organisms. Several component domains have been detec...

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Main Authors: Bhanupratap Chouhan, Alexander Denesyuk, Jyrki Heino, Mark S Johnson, Konstantin Denessiouk
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2011-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC3192720?pdf=render
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spelling doaj-5e4e29a464264eba9f1e5f8072d594ea2020-11-25T00:12:14ZengPublic Library of Science (PLoS)PLoS ONE1932-62032011-01-01610e2506910.1371/journal.pone.0025069Conservation of the human integrin-type beta-propeller domain in bacteria.Bhanupratap ChouhanAlexander DenesyukJyrki HeinoMark S JohnsonKonstantin DenessioukIntegrins are heterodimeric cell-surface receptors with key functions in cell-cell and cell-matrix adhesion. Integrin α and β subunits are present throughout the metazoans, but it is unclear whether the subunits predate the origin of multicellular organisms. Several component domains have been detected in bacteria, one of which, a specific 7-bladed β-propeller domain, is a unique feature of the integrin α subunits. Here, we describe a structure-derived motif, which incorporates key features of each blade from the X-ray structures of human αIIbβ3 and αVβ3, includes elements of the FG-GAP/Cage and Ca(2+)-binding motifs, and is specific only for the metazoan integrin domains. Separately, we searched for the metazoan integrin type β-propeller domains among all available sequences from bacteria and unicellular eukaryotic organisms, which must incorporate seven repeats, corresponding to the seven blades of the β-propeller domain, and so that the newly found structure-derived motif would exist in every repeat. As the result, among 47 available genomes of unicellular eukaryotes we could not find a single instance of seven repeats with the motif. Several sequences contained three repeats, a predicted transmembrane segment, and a short cytoplasmic motif associated with some integrins, but otherwise differ from the metazoan integrin α subunits. Among the available bacterial sequences, we found five examples containing seven sequential metazoan integrin-specific motifs within the seven repeats. The motifs differ in having one Ca(2+)-binding site per repeat, whereas metazoan integrins have three or four sites. The bacterial sequences are more conserved in terms of motif conservation and loop length, suggesting that the structure is more regular and compact than those example structures from human integrins. Although the bacterial examples are not full-length integrins, the full-length metazoan-type 7-bladed β-propeller domains are present, and sometimes two tandem copies are found.http://europepmc.org/articles/PMC3192720?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Bhanupratap Chouhan
Alexander Denesyuk
Jyrki Heino
Mark S Johnson
Konstantin Denessiouk
spellingShingle Bhanupratap Chouhan
Alexander Denesyuk
Jyrki Heino
Mark S Johnson
Konstantin Denessiouk
Conservation of the human integrin-type beta-propeller domain in bacteria.
PLoS ONE
author_facet Bhanupratap Chouhan
Alexander Denesyuk
Jyrki Heino
Mark S Johnson
Konstantin Denessiouk
author_sort Bhanupratap Chouhan
title Conservation of the human integrin-type beta-propeller domain in bacteria.
title_short Conservation of the human integrin-type beta-propeller domain in bacteria.
title_full Conservation of the human integrin-type beta-propeller domain in bacteria.
title_fullStr Conservation of the human integrin-type beta-propeller domain in bacteria.
title_full_unstemmed Conservation of the human integrin-type beta-propeller domain in bacteria.
title_sort conservation of the human integrin-type beta-propeller domain in bacteria.
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2011-01-01
description Integrins are heterodimeric cell-surface receptors with key functions in cell-cell and cell-matrix adhesion. Integrin α and β subunits are present throughout the metazoans, but it is unclear whether the subunits predate the origin of multicellular organisms. Several component domains have been detected in bacteria, one of which, a specific 7-bladed β-propeller domain, is a unique feature of the integrin α subunits. Here, we describe a structure-derived motif, which incorporates key features of each blade from the X-ray structures of human αIIbβ3 and αVβ3, includes elements of the FG-GAP/Cage and Ca(2+)-binding motifs, and is specific only for the metazoan integrin domains. Separately, we searched for the metazoan integrin type β-propeller domains among all available sequences from bacteria and unicellular eukaryotic organisms, which must incorporate seven repeats, corresponding to the seven blades of the β-propeller domain, and so that the newly found structure-derived motif would exist in every repeat. As the result, among 47 available genomes of unicellular eukaryotes we could not find a single instance of seven repeats with the motif. Several sequences contained three repeats, a predicted transmembrane segment, and a short cytoplasmic motif associated with some integrins, but otherwise differ from the metazoan integrin α subunits. Among the available bacterial sequences, we found five examples containing seven sequential metazoan integrin-specific motifs within the seven repeats. The motifs differ in having one Ca(2+)-binding site per repeat, whereas metazoan integrins have three or four sites. The bacterial sequences are more conserved in terms of motif conservation and loop length, suggesting that the structure is more regular and compact than those example structures from human integrins. Although the bacterial examples are not full-length integrins, the full-length metazoan-type 7-bladed β-propeller domains are present, and sometimes two tandem copies are found.
url http://europepmc.org/articles/PMC3192720?pdf=render
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