High-resolution FISH mapping of the rat α 2u -globulin multigene family

McFadyen, David A.; Locke, John

doi:10.1007/s003350010055

Cited by 8 publications

(3 citation statements)

References 35 publications

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“…1) may be an underestimate. The fact that the ␣-2-globulin cluster shows only five duplicated genes as opposed to the estimated 15-20 copies (McFadyen et al 1999;McFadyen and Locke 2000) may be a consequence of such an effect. Although many of the expected rat gene duplications and highly homologous gene families (i.e., carboxylesterases, ␣-2-globulin, cytochrome P450 genes, serine protease inhibitor, T-cell receptor, MHC genes, etc.…”

Section: Genome Research 501mentioning

confidence: 98%

Recent Segmental Duplications in the Working Draft Assembly of the Brown Norway Rat

Tüzün¹,

Bailey²,

Eichler³

2004

Genome Res.

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We assessed the content, structure, and distribution of segmental duplications (Ն90% sequence identity, Ն5 kb length) within the published version of the Rattus norvegicus genome assembly (v.3.1). The overall fraction of duplicated sequence within the rat assembly (2.92%) is greater than that of the mouse (1%-1.2%) but significantly less than that of human (∼5%). Duplications were nonuniformly distributed, occurring predominantly as tandem and tightly clustered intrachromosomal duplications. Regions containing extensive interchromosomal duplications were observed, particularly within subtelomeric and pericentromeric regions. We identified 41 discrete genomic regions greater than 1 Mb in size, termed "duplication blocks." These appear to have been the target of extensive duplication over millions of years of evolution. Gene content within duplicated regions (∼1%) was lower than expected based on the genome representation. Interestingly, sequence contigs lacking chromosome assignment ("the unplaced chromosome") showed a marked enrichment for segmental duplication (45% of 75.2 Mb), indicating that segmental duplications have been problematic for sequence and assembly of the rat genome. Further targeted efforts are required to resolve the organization and complexity of these regions.

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Section: Genome Research 501mentioning

confidence: 98%

Recent Segmental Duplications in the Working Draft Assembly of the Brown Norway Rat

Tüzün¹,

Bailey²,

Eichler³

2004

Genome Res.

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“…An increasing body of work, however, has demonstrated that the urinary proteins, which are ''hardwired'' into the genome of the donor animal, deliver highly complex relatively invariant signals in urine. Expression of these proteins is often sexually dimorphic, and in the major urinary proteins (MUPs), there is considerable polymorphism (Mucignat-Caretta et al 1995;Robertson et al 1996;McFadyen et al 1999;McFadyen and Locke 2000;Hurst et al 2001;Beynon et al 2002;Chamero et al 2007;Mudge et al 2008;Hurst and Beynon 2010). The involatility of proteins provides longevity against which the decay of more volatile signals can be measured (Darwish Marie et al 2001).…”

Section: Introductionmentioning

confidence: 99%

Roborovskin, a Lipocalin in the Urine of the Roborovski Hamster, Phodopus roborovskii

et al. 2010

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Many rodents are now known to exhibit an obligate proteinuria that delivers urine-mediated chemosignals. In this paper, we explore the urinary proteins of the Roborovski hamster (Phodopus roborovskii). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis of urine from individual male and female Roborovski hamsters revealed 2 proteins, with approximate masses of 6 and 17 kDa, the expression pattern of which showed little variation between individuals or between sexes. Peptide mass fingerprints obtained from these 2 proteins revealed a number of features: 1) the proteins of a given mass were the same in all individuals regardless of sex, 2) the 6 kDa protein was not a fragment of the 21 kDa protein, and 3) neither protein was a fragment of a larger, conserved protein such as serum albumin. Electrospray mass spectrometry of purified protein preparations established the mass of the larger protein as invariant, at 17144 ± 2 Da in all samples. This protein has been termed roborovskin. The primary structure of roborovskin was determined by tandem mass spectrometry of peptides derived from independent and overlapping digestion with 3 proteases, supported by Edman degradation of the protein N-terminus. Roborovskin shared significant homology with olfactory-binding proteins from Myodes glareolus (bank vole) and with aphrodisin and submandibular protein from the golden hamster Mesocricetus auratus, all of which belong to the lipocalin superfamily. Lower levels of homology were also indicated between a variety of other lipocalins including the major urinary proteins from house mice and Norway rats. A model of the tertiary structure of roborovskin was constructed from the primary sequence by homology modeling. This model structure resembled other 8-stranded beta barrel lipocalins. Thus, the Roborovski hamster may demonstrate another variant of urinary lipocalin expression, as for the animals studied here, there appears to be no polymorphism in expression either between sexes or individuals.

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“…edu), Ensembl (http://www.ensembl.org/Rattus_norvegicus/ Info/Index), NCBI (http://www.ncbi.nlm.nih.gov/genome/ 73) and UCSC (http://genome-euro.ucsc.edu/). Manual annotation performed by Logan and colleagues on the previous release (Rnor_3.4) shows that there are a minimum of nine genes and 13 pseudogenes [17], in good agreement with Southern blot [20] and fluorescence in situ hybridization [21] analysis. The rat genes do not seem to be grouped into different regions, and all genes have sequence similarity of approximately 90 % ( Figure 1).…”

Section: The Mup Gene Clustermentioning

confidence: 80%

The major urinary protein system in the rat

Gómez‐Baena

Armstrong

Phelan

et al. 2014

Biochemical Society Transactions

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The genomes of rats and mice both contain a cluster of multiple genes that encode small (18-20 kDa) eight-stranded β-barrel lipocalins that are expressed in multiple secretory tissues, some of which enter urine via hepatic biosynthesis. These proteins have been given different names, but are mostly generically referred to as MUPs (major urinary proteins). The mouse MUP cluster is increasingly well understood, and, in particular, a number of roles for MUPs in chemical communication between conspecifics have been established. By contrast, the literature on the rat orthologues is much less well developed and is fragmented. In the present review, we summarize current knowledge on the MUPs from the Norway (or brown) rat, Rattus norvegicus.

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High-resolution FISH mapping of the rat α 2u -globulin multigene family

Cited by 8 publications

References 35 publications

Recent Segmental Duplications in the Working Draft Assembly of the Brown Norway Rat

Recent Segmental Duplications in the Working Draft Assembly of the Brown Norway Rat

Roborovskin, a Lipocalin in the Urine of the Roborovski Hamster, Phodopus roborovskii

The major urinary protein system in the rat

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