Structure and chromosome localization of the human eosinophil-derived neurotoxin and eosinophil cationic protein genes: Evidence for intronless coding sequences in the ribonuclease gene superfamily

Hamann, Kimm J.; Ten, Rosa M.; Loegering, David A.; Jenkins, Robert B.; Heise, Mark T.; Schad, Christopher R.; Pease, Larry R.; Gleich, Gerald J.; Barker, Robert L.

doi:10.1016/0888-7543(90)90197-3

Cited by 98 publications

(66 citation statements)

References 47 publications

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“…This protein was subsequently shown to contain RNase activity and to be structurally homologous to bovine pancreatic RNase A (Gleich et al, 1986;Slifman et al, 1986). Its amino acid sequence, deduced from the DNA sequence (Hamann et al, 1990), is identical to the chemically determined sequence of RNase Us found in human urine (Beintema et al, 1988), except for the amino acid residue at position 7. Whereas a tryptophan residue was predicted from the DNA sequence of EDN, this amino acid could not be identified by chemical means in RNase Us (Beintema et al, 1988) or in EDN (Gleich et al, 1986).…”

mentioning

confidence: 72%

New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us

Hofsteenge¹,

Müller²,

Beer³

et al. 1994

Biochemistry

270

234

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We report a new type of linkage between a carbohydrate and a protein, involving the rarely modified side chain of a tryptophan residue. An aldohexopyranosyl residue was found to be linked via a C-C bond to the indole ring of the tryptophan residue at position 7 of human RNase Us. Mass spectrometric analysis of peptides containing this residue showed a molecular mass 162 Da higher than that expected for tryptophan. The fragmentation pattern of the modified amino acid side chain was reminiscent of that of aromatic C-glycosides, suggesting a direct attachment of a hexose residue to a C-position of the tryptophan indole moiety. 'H and 13C NMR spectroscopic data confirmed this inference and unequivocally demonstrated the substituent to be an aldohexopyranosyl residue, C-glycosidically linked to the C2 atom of the indole. This mode of attachment differs from the ones known so far, in which carbohydrates are linked to an amino acid side chain by N-or 0-glycosidic bonds.

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mentioning

confidence: 72%

New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us

Hofsteenge¹,

Müller²,

Beer³

et al. 1994

Biochemistry

270

234

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“…ECP and EDN are RNase genes that arose about 31 million years ago through a gene duplication event in the ancestor to Old World monkeys and hominoids (Hamann et al 1990;Zhang et al 1998). Both ECP and EDN have host-defense roles, but their specific functions differ.…”

Section: Ecp and Ednmentioning

confidence: 99%

A Maximum Likelihood Method for Detecting Functional Divergence at Individual Codon Sites, with Application to Gene Family Evolution

2004

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Abstract. The tailoring of existing genetic systems to new uses is called genetic co-option. Mechanisms of genetic co-option have been difficult to study because of difficulties in identifying functionally important changes. One way to study genetic co-option in protein-coding genes is to identify those amino acid sites that have experienced changes in selective pressure following a genetic co-option event. In this paper we present a maximum likelihood method useful for measuring divergent selective pressures and identifying the amino acid sites affected by divergent selection. The method is based on a codon model of evolution and uses the nonsynonymous-to-synonymous rate ratio (x) as a measure of selection on the protein, with x = 1, <1, and >1 indicating neutral evolution, purifying selection, and positive selection, respectively. The model allows variation in x among sites, with a fraction of sites evolving under divergent selective pressures. Divergent selection is indicated by different x's between clades, such as between paralogous clades of a gene family. We applied the codon model to duplication followed by functional divergence of (i) the e and c globin genes and (ii) the eosinophil cationic protein (ECP) and eosinophilderived neurotoxin (EDN) genes. In both cases likelihood ratio tests suggested the presence of sites evolving under divergent selective pressures. Results of the e and c globin analysis suggested that divergent selective pressures might be a consequence of a weakened relationship between fetal hemoglobin and 2,3-diphosphoglycerate. We suggest that empirical Bayesian identification of sites evolving under divergent selective pressures, combined with structural and functional information, can provide a valuable framework for identifying and studying mechanisms of genetic co-option. Limitations of the new method are discussed.

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“…In human, the eosinophil-expressed subfamily expanded through two lineage-specific duplications to give rise to RNASE2 (eosinophil-derived neurotoxin), RNASE3 (eosinophil cationic protein; Hamann et al 1990), and ECRP (GenBank X55989). Multiple mouse-specific duplications produced at least six genes (Ear-1, Ear-2, and mR-3 through mR-6; Batten et al 1997).…”

Section: Eosinophil-associated Ribonucleasesmentioning

confidence: 99%

Divergence of Spatial Gene Expression Profiles Following Species-Specific Gene Duplications in Human and Mouse

Huminiecki

Wolfe²

2004

Genome Res.

149

128

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To examine the process by which duplicated genes diverge in function, we studied how the gene expression profiles of orthologous gene sets in human and mouse are affected by the presence of additional recent species-specific paralogs. Gene expression profiles were compared across 16 homologous tissues in human and mouse using microarray data from the Gene Expression Atlas for 1575 sets of orthologs including 250 with species-specific paralogs. We find that orthologs that have undergone recent duplication are less likely to have strongly correlated expression profiles than those that remain in a one-to-one relationship between human and mouse. There is a general trend for paralogous genes to become more specialized in their expression patterns, with decreased breadth and increased specificity of expression as gene family size increases. Despite this trend, detailed examination of some particular gene families where species-specific duplications have occurred indicated several examples of apparent neofunctionalization of duplicated genes, but only one case of subfunctionalization. Often, the expression of both copies of a duplicated gene appears to have changed relative to the ancestral state. Our results suggest that gene expression profiles are surprisingly labile and that expression in a particular tissue may be gained or lost repeatedly during the evolution of even small gene families. We conclude that gene duplication is a major driving force behind the emergence of divergent gene expression patterns

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Structure and chromosome localization of the human eosinophil-derived neurotoxin and eosinophil cationic protein genes: Evidence for intronless coding sequences in the ribonuclease gene superfamily

Cited by 98 publications

References 47 publications

New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us

New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us

A Maximum Likelihood Method for Detecting Functional Divergence at Individual Codon Sites, with Application to Gene Family Evolution

Divergence of Spatial Gene Expression Profiles Following Species-Specific Gene Duplications in Human and Mouse

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