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The Skeleton Forming Proteome of an Early Branching Metazoan: A Molecular Survey of the Biomineralization Components Employed by the Coralline Sponge Vaceletia Sp.

Germer J, Mann K, Wörheide G, Jackson DJ - PLoS ONE (2015)

Bottom Line: Very few biomineralization associated proteins have been identified in sponges so far, with no transcriptome or proteome scale surveys yet available.Among these proteins are known biomineralization compounds, such as carbonic anhydrase, spherulin, extracellular matrix proteins and very acidic proteins.However, lineage specific evolution is also likely to have contributed significantly to the ability of disparate metazoan lineages to biocalcify.

View Article: PubMed Central - PubMed

Affiliation: Department of Geobiology, Georg-August University of Göttingen, Göttingen, Germany.

ABSTRACT
The ability to construct a mineralized skeleton was a major innovation for the Metazoa during their evolution in the late Precambrian/early Cambrian. Porifera (sponges) hold an informative position for efforts aimed at unraveling the origins of this ability because they are widely regarded to be the earliest branching metazoans, and are among the first multi-cellular animals to display the ability to biomineralize in the fossil record. Very few biomineralization associated proteins have been identified in sponges so far, with no transcriptome or proteome scale surveys yet available. In order to understand what genetic repertoire may have been present in the last common ancestor of the Metazoa (LCAM), and that may have contributed to the evolution of the ability to biocalcify, we have studied the skeletal proteome of the coralline demosponge Vaceletia sp. and compare this to other metazoan biomineralizing proteomes. We bring some spatial resolution to this analysis by dividing Vaceletia's aragonitic calcium carbonate skeleton into "head" and "stalk" regions. With our approach we were able to identify 40 proteins from both the head and stalk regions, with many of these sharing some similarity to previously identified gene products from other organisms. Among these proteins are known biomineralization compounds, such as carbonic anhydrase, spherulin, extracellular matrix proteins and very acidic proteins. This report provides the first proteome scale analysis of a calcified poriferan skeletal proteome, and its composition clearly demonstrates that the LCAM contributed several key enzymes and matrix proteins to its descendants that supported the metazoan ability to biocalcify. However, lineage specific evolution is also likely to have contributed significantly to the ability of disparate metazoan lineages to biocalcify.

No MeSH data available.


Related in: MedlinePlus

Schematic representation of Vaceletia sp. head and stalk region with iBAQ estimates of protein abundances.12 proteins are enriched in the head, while 7 proteins are enriched in the stalk and 21 proteins have an equal abundance in head and stalk. Protein abundances were considered as different when iBAQ estimations between head and stalk were ≥ 0.5. Proteins in bold were only detected in the head proteome.
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pone.0140100.g004: Schematic representation of Vaceletia sp. head and stalk region with iBAQ estimates of protein abundances.12 proteins are enriched in the head, while 7 proteins are enriched in the stalk and 21 proteins have an equal abundance in head and stalk. Protein abundances were considered as different when iBAQ estimations between head and stalk were ≥ 0.5. Proteins in bold were only detected in the head proteome.

Mentions: All proteins identified in the stalk were present in the head, but some proteins identified in the head were unique to that location. Based on iBAQ values that yield the percentages of proteins normalized to the sum of iBAQ intensities of all identified proteins in a sample, 40 of the 121 identified head proteins constitute more than 90% of the total identified head proteome and 35 of the 72 identified stalk proteins (all of which are present in the head proteome) constitute more than 87% of the stalk total identified proteome (Table 1). We will only consider these 40 "major" proteins further as they are likely to represent the key components of Vaceletia's biomineral proteome, however all 122 isotigs (consisting of 181 contigs) are provided in S1 File. In general the majority of these proteins share similarity with proteins in UniProt and/or contain recognizable protein domains (Table 1); eleven of the 40 most abundant proteins did not return hits against UniProt. Of these 40 major proteins approximately 50% apparently differ in their abundance within the head and stalk regions (19 out of 40; Fig 4).


The Skeleton Forming Proteome of an Early Branching Metazoan: A Molecular Survey of the Biomineralization Components Employed by the Coralline Sponge Vaceletia Sp.

Germer J, Mann K, Wörheide G, Jackson DJ - PLoS ONE (2015)

Schematic representation of Vaceletia sp. head and stalk region with iBAQ estimates of protein abundances.12 proteins are enriched in the head, while 7 proteins are enriched in the stalk and 21 proteins have an equal abundance in head and stalk. Protein abundances were considered as different when iBAQ estimations between head and stalk were ≥ 0.5. Proteins in bold were only detected in the head proteome.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4633127&req=5

pone.0140100.g004: Schematic representation of Vaceletia sp. head and stalk region with iBAQ estimates of protein abundances.12 proteins are enriched in the head, while 7 proteins are enriched in the stalk and 21 proteins have an equal abundance in head and stalk. Protein abundances were considered as different when iBAQ estimations between head and stalk were ≥ 0.5. Proteins in bold were only detected in the head proteome.
Mentions: All proteins identified in the stalk were present in the head, but some proteins identified in the head were unique to that location. Based on iBAQ values that yield the percentages of proteins normalized to the sum of iBAQ intensities of all identified proteins in a sample, 40 of the 121 identified head proteins constitute more than 90% of the total identified head proteome and 35 of the 72 identified stalk proteins (all of which are present in the head proteome) constitute more than 87% of the stalk total identified proteome (Table 1). We will only consider these 40 "major" proteins further as they are likely to represent the key components of Vaceletia's biomineral proteome, however all 122 isotigs (consisting of 181 contigs) are provided in S1 File. In general the majority of these proteins share similarity with proteins in UniProt and/or contain recognizable protein domains (Table 1); eleven of the 40 most abundant proteins did not return hits against UniProt. Of these 40 major proteins approximately 50% apparently differ in their abundance within the head and stalk regions (19 out of 40; Fig 4).

Bottom Line: Very few biomineralization associated proteins have been identified in sponges so far, with no transcriptome or proteome scale surveys yet available.Among these proteins are known biomineralization compounds, such as carbonic anhydrase, spherulin, extracellular matrix proteins and very acidic proteins.However, lineage specific evolution is also likely to have contributed significantly to the ability of disparate metazoan lineages to biocalcify.

View Article: PubMed Central - PubMed

Affiliation: Department of Geobiology, Georg-August University of Göttingen, Göttingen, Germany.

ABSTRACT
The ability to construct a mineralized skeleton was a major innovation for the Metazoa during their evolution in the late Precambrian/early Cambrian. Porifera (sponges) hold an informative position for efforts aimed at unraveling the origins of this ability because they are widely regarded to be the earliest branching metazoans, and are among the first multi-cellular animals to display the ability to biomineralize in the fossil record. Very few biomineralization associated proteins have been identified in sponges so far, with no transcriptome or proteome scale surveys yet available. In order to understand what genetic repertoire may have been present in the last common ancestor of the Metazoa (LCAM), and that may have contributed to the evolution of the ability to biocalcify, we have studied the skeletal proteome of the coralline demosponge Vaceletia sp. and compare this to other metazoan biomineralizing proteomes. We bring some spatial resolution to this analysis by dividing Vaceletia's aragonitic calcium carbonate skeleton into "head" and "stalk" regions. With our approach we were able to identify 40 proteins from both the head and stalk regions, with many of these sharing some similarity to previously identified gene products from other organisms. Among these proteins are known biomineralization compounds, such as carbonic anhydrase, spherulin, extracellular matrix proteins and very acidic proteins. This report provides the first proteome scale analysis of a calcified poriferan skeletal proteome, and its composition clearly demonstrates that the LCAM contributed several key enzymes and matrix proteins to its descendants that supported the metazoan ability to biocalcify. However, lineage specific evolution is also likely to have contributed significantly to the ability of disparate metazoan lineages to biocalcify.

No MeSH data available.


Related in: MedlinePlus