CRTAC1 homolog proteins are conserved from cyanobacteria to man and secreted by the teleost fish pituitary gland

Redruello, Begoña; Louro, Bruno; Anjos, Liliana; Silva, Nádia; Greenwell, Roger; Canário, Adelino V.M.; Power, Deborah M.

doi:10.1016/j.gene.2010.02.003

Cited by 12 publications

(15 citation statements)

References 35 publications

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“…The N ‐terminal domain of CRTAC1 includes seven phenylalanyl‐glycyl‐glycyl‐alanyl‐prolyl (FG‐GAP) amino acid repeats forming a β‐strand rich region that is associated with beta‐propeller structures. This supports the notion that CRTAC1 has a seven‐bladed beta‐propeller structure as previously suggested . Proteins with a beta‐propeller fold are especially interesting because of their extreme sequence/function and phylogenetic diversity despite their similar three‐dimensional fold .…”

Section: Introductionsupporting

confidence: 89%

“…In teleost fish, the teleost specific whole genome duplication generated two homologue genes, crtac1a and crtac1b , that in the few teleost species examined so far have been retained. The two forms of teleost Crtac1 share high amino acid sequence conservation with the exception of the C‐terminal EGF‐Like calcium binding motif that is specific to Crtac1a . The sea bream Crtac1b (saCrtac1b) protein is hyperthermostable and both recombinant and tissue‐derived proteins have a high propensity to form large aggregates .…”

Section: Introductionmentioning

confidence: 99%

“…In this study, we update the evolutionary analysis of the CRTAC1 gene and explore the structural and biochemical modifications that occurred during CRTAC1 evolution and their influence on its aggregation potential . Using a comparative approach, we explore the unique divergent character of teleost duplicate Crtac1's and human CRTAC1 and examine their stability and biochemical properties.…”

Section: Introductionmentioning

confidence: 99%

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Cartilage acidic protein 1, a new member of the beta-propeller protein family with amyloid propensity

et al. 2016

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Cartilage acidic protein1 (CRTAC1) is an extracellular matrix protein of chondrogenic tissue in humans and its presence in bacteria indicate it is of ancient origin. Structural modeling of piscine CRTAC1 reveals it belongs to the large family of beta-propeller proteins that in mammals have been associated with diseases, including amyloid diseases such as Alzheimer's. In order to characterize the structure/function evolution of this new member of the beta-propeller family we exploited the unique characteristics of piscine duplicate genes Crtac1a and Crtac1b and compared their structural and biochemical modifications with human recombinant CRTAC1. We demonstrate that CRTAC1 has a beta-propeller structure that has been conserved during evolution and easily forms high molecular weight thermo-stable aggregates. We reveal for the first time the propensity of CRTAC1 to form amyloid-like structures, and hypothesize that the aggregating property of CRTAC1 may be related to its disease-association. We further contribute to the general understating of CRTAC1's and beta-propeller family evolution and function. Proteins 2017; 85:242-255. © 2016 Wiley Periodicals, Inc.

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Section: Introductionsupporting

confidence: 89%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Cartilage acidic protein 1, a new member of the beta-propeller protein family with amyloid propensity

et al. 2016

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“…This prompted us to search for further instances of this type of Dx[DN]xDG motif in the human genome. Using the results of the iterative database searches described above various integrins and integrin-like proteins were retrieved, as expected, along with the related domains known to be present in phosphatidylinositol -specific phospholipase D [41] and the motifs recently described in cartilage acidic protein [42]. Three novel proteins containing two motifs each (Table 2) were also recovered with significant e-values; proteins that were independently confirmed to be β-propellers by profile-profile matching.…”

Section: Resultsmentioning

confidence: 97%

New Structural and Functional Contexts of the Dx[DN]xDG Linear Motif: Insights into Evolution of Calcium-Binding Proteins

et al. 2011

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Binding of calcium ions (Ca2+) to proteins can have profound effects on their structure and function. Common roles of calcium binding include structure stabilization and regulation of activity. It is known that diverse families – EF-hands being one of at least twelve – use a Dx[DN]xDG linear motif to bind calcium in near-identical fashion. Here, four novel structural contexts for the motif are described. Existing experimental data for one of them, a thermophilic archaeal subtilisin, demonstrate for the first time a role for Dx[DN]xDG-bound calcium in protein folding. An integrin-like embedding of the motif in the blade of a β-propeller fold – here named the calcium blade – is discovered in structures of bacterial and fungal proteins. Furthermore, sensitive database searches suggest a common origin for the calcium blade in β-propeller structures of different sizes and a pan-kingdom distribution of these proteins. Factors favouring the multiple convergent evolution of the motif appear to include its general Asp-richness, the regular spacing of the Asp residues and the fact that change of Asp into Gly and vice versa can occur though a single nucleotide change. Among the known structural contexts for the Dx[DN]xDG motif, only the calcium blade and the EF-hand are currently found intracellularly in large numbers, perhaps because the higher extracellular concentration of Ca2+ allows for easier fixing of newly evolved motifs that have acquired useful functions. The analysis presented here will inform ongoing efforts toward prediction of similar calcium-binding motifs from sequence information alone.

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“…** p < 0.01 versus H1 control. D–F Examples of E11 cortical cells transduced with Ebf2 shRNA, Ebf2 overexpression constructs or the control H1 lentivirus (indicated by EGFP) that were stained for Reelin [54]. Arrows indicate some Reelin + cells.…”

Section: Resultsmentioning

confidence: 99%

Ebf2 Marks Early Cortical Neurogenesis and Regulates the Generation of Cajal-Retzius Neurons in the Developing Cerebral Cortex

Chuang¹,

Wang

et al. 2011

Dev Neurosci

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Mammalian cortical neurogenesis occurs on a precise time schedule during development. The earliest born neurons form the preplate and later separate into layer 1, which includes Cajal-Retzius (C-R) neurons, and the subplate. The preplate and its derivatives play a critical role in regulating subsequent neuron migration and cortical lamination. Using an early B cell factor 2 (Ebf2)-enhanced green fluorescent protein (EGFP) transgenic mouse line, we show that Ebf2-EGFP is expressed in the preplate and persists in C-R neurons, allowing us to follow the development of these early born neurons. Therefore, Ebf2 is a genetic marker for preplate neurons from the earliest stage of their differentiation and C-R cells after the preplate is split. Additionally, we examined the function of Ebf2 in the development of C-R neurons using both lentiviral-mediated knock-down overexpression approaches to perturb Ebf2 expression. Our data show that Ebf2 overexpression increases the generation of early born neurons including C-R cells, while Ebf2 knock-down decreases it, without affecting the generation of other layer-specific neurons in vitro. These results indicate that Ebf2 is important for early cortical neurogenesis and regulates the generation of C-R neurons in the developing cerebral cortex.

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CRTAC1 homolog proteins are conserved from cyanobacteria to man and secreted by the teleost fish pituitary gland

Cited by 12 publications

References 35 publications

Cartilage acidic protein 1, a new member of the beta-propeller protein family with amyloid propensity

Cartilage acidic protein 1, a new member of the beta-propeller protein family with amyloid propensity

New Structural and Functional Contexts of the Dx[DN]xDG Linear Motif: Insights into Evolution of Calcium-Binding Proteins

Ebf2 Marks Early Cortical Neurogenesis and Regulates the Generation of Cajal-Retzius Neurons in the Developing Cerebral Cortex

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