scholarly journals Patterns of urine scent mark pheromone evolution in house mice and relatives (Muridae:Mus)

2019 ◽  
Author(s):  
Michael J Sheehan ◽  
Polly Campbell ◽  
Caitlin H Miller
Keyword(s):  
Sexual Selection ◽  
Amino Acid ◽  
Protein Product ◽  
House Mice ◽  
Scent Mark ◽  
Individual Identity ◽  
Scent Marks ◽  
Major Urinary Proteins ◽  
Pheromone Evolution ◽  
Amino Acid Variants

ABSTRACTScent marks are important mediators of territorial behavior and sexual selection in many species, especially among mammals. As such, the evolution of compounds used in scent marks has the potential to inform our understanding of signal evolution in relation to social and sexual selection. A major challenge in studies of chemical communication is that the link between semiochemical compounds and genetic changes is often unclear. The major urinary proteins (MUPs) of house mice are elaborated pheromone blends that provide information on sex, status and individual identity. Importantly, MUPs are a direct protein product of genes, providing a clear link between genotype and phenotype. Here we examine the evolution of urinary pheromone signals among house mice and relatives by examining the sequences and patterns of expression of MUPs in the liver, where urine excreted MUPs are produced. MUP patterns have evolved among mouse species both by gene duplication and variation in expression. Notably, the sex-specificity of pheromone expression that has previously been assumed to be male-specific varies considerably across species. Our data reveal that individual identity signals in MUPs evolved prior to 0.35 million years ago and have rapidly diversified through recombining a modest number of perceptually salient amino acid variants. Amino acid variants are much more common on the exterior of the protein where they could interact with vomeronasal receptors, suggesting that perception have played a major role in shaping MUP diversity. Collectively, these data provide new insights into the diverse processes and pressures shaping pheromone signals, and suggest new avenues for using house mice and their wild relatives to probe the evolution of signals and signal processing.

scholarly journals Wake up and smell the conflict: odour signals in female competition

2013 ◽  
Vol 368 (1631) ◽  
pp. 20130082 ◽  
Author(s):  
Paula Stockley ◽  
Lisa Bottell ◽  
Jane L. Hurst
Keyword(s):  
Competitive Ability ◽  
Scent Marking ◽  
House Mice ◽  
Scent Mark ◽  
Female Competition ◽  
Scent Marks ◽  
Natural Conditions ◽  
Major Urinary Protein ◽  
Aggressive Interactions ◽  
Female Ornaments

Odour signals used in competitive and aggressive interactions between males are well studied in the context of sexual selection. By contrast, relatively little is known about comparable signals used by females, despite current interest in the evolution of female ornaments and weaponry. Available evidence suggests that odour signals are important in competitive interactions between female mammals, with reductions or reversals of male-biased sexual dimorphism in signalling where female competition is intense. Scent marking is often associated with conflict between females over access to resources or reproductive opportunities. Female scent marks may therefore provide reliable signals of competitive ability that could be used both by competitors and potential mates. Consistent with this hypothesis, we report that aggressive behaviour of female house mice is correlated with the amount of major urinary protein (MUP) excreted in their urine, a polymorphic set of proteins that are used in scent mark signalling. Under semi-natural conditions, females with high MUP output are more likely to produce offspring sired by males that have high reproductive success, and less likely to produce offspring by multiple different sires, suggesting that females with strong MUP signals are monopolized by males of particularly high quality. We conclude that odour signals are worthy of more detailed investigation as mediators of female competition.

scholarly journals Pheromones that Correlate with Reproductive Success in Competitive Conditions

2021 ◽  
Author(s):  
Kenneth C. Luzynski ◽  
Doris Nicolakis ◽  
Maria Adelaide Marconi ◽  
Sarah M. Zala ◽  
Jae Kwak ◽  
...  
Keyword(s):  
Reproductive Success ◽  
Social Status ◽  
Protein Concentration ◽  
Urinary Protein ◽  
House Mice ◽  
Male Reproductive Success ◽  
Urinary Proteins ◽  
Scent Marks ◽  
Major Urinary Proteins ◽  
Volatile Organic

Abstract The major urinary proteins (MUPs) of house mice (Mus musculus) bind and stabilize the release of pheromones and other volatile organic compounds (VOCs) from urinary scent marks, which mediate chemical communication. Social status influences MUP and VOC excretion, and the urinary scent of dominant males is attractive to females. Urinary pheromones influence the sexual behavior and physiology of conspecifics, and yet it is not known whether they also affect reproductive success. We monitored the excretion of urinary protein and VOCs of wild-derived house mice living in large seminatural enclosures to compare the sexes and to test how these compounds correlate with reproductive success. Among males, urinary protein concentration and VOC expression correlated with reproductive success and social status. Territorial dominance also correlated with reproductive success in both sexes; but among females, no urinary compounds were found to correlate with social status or reproductive success. Notably, the large sex differences in chemosensory compounds found in laboratory studies were significantly lower when the mice lived in seminatural conditions. These findings provide novel evidence for chemical signals that correlate with male reproductive success of house mice living in competitive conditions.

scholarly journals Lymphocytic Choriomeningitis Virus Alters the Expression of Male Mouse Scent Proteins

Viruses ◽  
2021 ◽  
Vol 13 (6) ◽  
pp. 1180
Author(s):  
Michael B. A. Oldstone ◽  
Brian C. Ware ◽  
Amanda Davidson ◽  
Mark C. Prescott ◽  
Robert J. Beynon ◽  
...  
Keyword(s):  
Mate Selection ◽  
Lymphocytic Choriomeningitis ◽  
T Cell Response ◽  
Mature Male ◽  
Cytotoxic T Cell ◽  
Scent Marks ◽  
High Concentration ◽  
Embryo Survival ◽  
Major Urinary Proteins ◽  
The Individual

Mature male mice produce a particularly high concentration of major urinary proteins (MUPs) in their scent marks that provide identity and status information to conspecifics. Darcin (MUP20) is inherently attractive to females and, by inducing rapid associative learning, leads to specific attraction to the individual male’s odour and location. Other polymorphic central MUPs, produced at much higher abundance, bind volatile ligands that are slowly released from a male’s scent marks, forming the male’s individual odour that females learn. Here, we show that infection of C57BL/6 males with LCMV WE variants (v2.2 or v54) alters MUP expression according to a male’s infection status and ability to clear the virus. MUP output is substantially reduced during acute adult infection with LCMV WE v2.2 and when males are persistently infected with LCMV WE v2.2 or v54. Infection differentially alters expression of darcin and, particularly, suppresses expression of a male’s central MUP signature. However, following clearance of acute v2.2 infection through a robust virus-specific CD8 cytotoxic T cell response that leads to immunity to the virus, males regain their normal mature male MUP pattern and exhibit enhanced MUP output by 30 days post-infection relative to uninfected controls. We discuss the likely impact of these changes in male MUP signals on female attraction and mate selection. As LCMV infection during pregnancy can substantially reduce embryo survival and lead to lifelong infection in surviving offspring, we speculate that females use LCMV-induced changes in MUP expression both to avoid direct infection from a male and to select mates able to develop immunity to local variants that will be inherited by their offspring.

scholarly journals The Role of Arg13 in Protein Phosphatase M tPphA from Thermosynechococcus elongatus

2012 ◽  
Vol 2012 ◽  
pp. 1-7 ◽  
Author(s):  
Jiyong Su ◽  
Karl Forchhammer
Keyword(s):  
Amino Acid ◽  
Protein Phosphatase ◽  
Arginine Residue ◽  
Side Chain ◽  
Wild Type ◽  
Catalytic Center ◽  
Nitrophenyl Phosphate ◽  
Reduced Activity ◽  
Amino Acid Variants

A highly conserved arginine residue is close to the catalytic center of PPM/PP2C-type protein phosphatases. Different crystal structures of PPM/PP2C homologues revealed that the guanidinium side chain of this arginine residue can adopt variable conformations and may bind ligands, suggesting an important role of this residue during catalysis. In this paper, we randomly mutated Arginine 13 of tPphA, a PPM/PP2C-type phosphatase from Thermosynechococcus elongatus, and obtained 18 different amino acid variants. The generated variants were tested towards p-nitrophenyl phosphate and various phosphopeptides. Towards p-nitrophenyl phosphate as substrate, twelve variants showed 3–7 times higher Km values than wild-type tPphA and four variants (R13D, R13F, R13L, and R13W) completely lost activity. Strikingly, these variants were still able to dephosphorylate phosphopeptides, although with strongly reduced activity. The specific inability of some Arg-13 variants to hydrolyze p-nitrophenyl phosphate highlights the importance of additional substrate interactions apart from the substrate phosphate for catalysis. The properties of the R13 variants indicate that this residue assists in substrate binding.

Heterogeneity of Major Urinary Proteins in House Mice: Population and Sex Differences

2001 ◽  
pp. 233-240 ◽  
Author(s):  
Caroline E. Payne ◽  
Nick Malone ◽  
Rick Humphries ◽  
Carl Bradbrook ◽  
Christina Veggerby ◽  
...  
Keyword(s):  
Sex Differences ◽  
House Mice ◽  
Urinary Proteins ◽  
Major Urinary Proteins

scholarly journals Multiple Advantageous Amino Acid Variants in the NAT2 Gene in Human Populations

PLoS ONE ◽  
2008 ◽  
Vol 3 (9) ◽  
pp. e3136 ◽  
Author(s):  
Francesca Luca ◽  
Giuseppina Bubba ◽  
Massimo Basile ◽  
Radim Brdicka ◽  
Emmanuel Michalodimitrakis ◽  
...  
Keyword(s):  
Amino Acid ◽  
Human Populations ◽  
Nat2 Gene ◽  
Amino Acid Variants

scholarly journals Diversity of major urinary proteins (MUPs) in wild house mice

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Michaela Thoß ◽  
Viktoria Enk ◽  
Hans Yu ◽  
Ingrid Miller ◽  
Kenneth C. Luzynski ◽  
...  
Keyword(s):  
House Mice ◽  
Urinary Proteins ◽  
Major Urinary Proteins ◽  
Wild House Mice

scholarly journals MaveRegistry: a collaboration platform for multiplexed assays of variant effect

2020 ◽  
Author(s):  
Da Kuang ◽  
Jochen Weile ◽  
Nishka Kishore ◽  
Alan F. Rubin ◽  
Stanley Fields ◽  
...  
Keyword(s):  
Amino Acid ◽  
International Community ◽  
Human Variation ◽  
Single Nucleotide ◽  
Clinical Interpretation ◽  
Link Type ◽  
Variant Effect ◽  
Genomic Regions ◽  
Amino Acid Variants

AbstractSummaryMultiplexed assays of variant effect (MAVEs) are capable of experimentally testing all possible single nucleotide or amino acid variants in selected genomic regions, generating ‘variant effect maps’, which provide biochemical insight and functional evidence to enable more rapid and accurate clinical interpretation of human variation. Because the international community applying MAVE approaches is growing rapidly, we developed the online MaveRegistry platform to catalyze collaboration, reduce redundant efforts, allow stakeholders to nominate targets, and enable tracking and sharing of progress on ongoing MAVE projects.Availability and implementationhttps://[email protected]

Protein truncation is required for the activation of the c-myb proto-oncogene

1991 ◽  
Vol 11 (8) ◽  
pp. 3987-3996
Author(s):  
F A Grässer ◽  
T Graf ◽  
J S Lipsick
Keyword(s):  
Amino Acid ◽  
Bone Marrow Cells ◽  
Protein Product ◽  
Full Length ◽  
Carboxyl Terminus ◽  
Amino Acid Substitutions ◽  
Amino Acid Residues ◽  
Avian Myeloblastosis Virus ◽  
Virally Encoded ◽  
Myb Proteins

The protein product of the v-myb oncogene of avian myeloblastosis virus, v-Myb, differs from its normal cellular counterpart, c-Myb, by (i) expression under the control of a strong viral long terminal repeat, (ii) truncation of both its amino and carboxyl termini, (iii) replacement of these termini by virally encoded residues, and (iv) substitution of 11 amino acid residues. We had previously shown that neither the virally encoded termini nor the amino acid substitutions are required for transformation by v-Myb. We have now constructed avian retroviruses that express full-length or singly truncated forms of c-Myb and have tested them for the transformation of chicken bone marrow cells. We conclude that truncation of either the amino or carboxyl terminus of c-Myb is sufficient for transformation. In contrast, the overexpression of full-length c-Myb does not result in transformation. We have also shown that the amino acid substitutions of v-Myb by themselves are not sufficient for the activation of c-Myb. Rather, the presence of either the normal amino or carboxyl terminus of c-Myb can suppress transformation when fused to v-Myb. Cells transformed by c-Myb proteins truncated at either their amino or carboxyl terminus appear to be granulated promyelocytes that express the Mim-1 protein. Cells transformed by a doubly truncated c-Myb protein are not granulated but do express the Mim-1 protein, in contrast to monoblasts transformed by v-Myb that neither contain granules nor express Mim-1. These results suggest that various alterations of c-Myb itself may determine the lineage of differentiating hematopoietic cells.

scholarly journals Molecular Analysis of the Rebeccamycin l-Amino Acid Oxidase from Lechevalieria aerocolonigenes ATCC 39243

2005 ◽  
Vol 187 (6) ◽  
pp. 2084-2092 ◽  
Author(s):  
Tomoyasu Nishizawa ◽  
Courtney C. Aldrich ◽  
David H. Sherman
Keyword(s):  
Amino Acid ◽  
Biochemical Characterization ◽  
Kinetic Studies ◽  
Biochemical Properties ◽  
Protein Product ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Left Hand ◽  
Key Enzyme ◽  
Hand Region

ABSTRACT Rebeccamycin, a member of the tryptophan-derived indolocarbazole family, is produced by Lechevalieria aerocolonigenes ATCC 39243. The biosynthetic pathway that specifies biosynthesis of this important metabolite is comprised of 11 genes spanning 18 kb of DNA. A presumed early enzyme involved in elaboration of the rebeccamycin aglycone is encoded by rebO, located at the left-hand region of the reb gene cluster. The deduced protein product, RebO (51.9 kDa), is an l-amino acid oxidase (l-AAO) that has 27% identity to an l-AAO from Scomber japonicus (animal, mackerel) and is a member of the family of FAD-dependent oxidase enzymes. In order to study the biochemical properties of this key enzyme, the rebO gene was overexpressed and purified from Escherichia coli. Biochemical characterization showed that RebO is dimeric, with a molecular mass of approximately 101 kDa. Further analysis revealed that the enzyme contains a noncovalently bound FAD cofactor and is reoxidized at the expense of molecular oxygen by producing one molecule of hydrogen peroxide. Based on kinetic studies, RebO shows significant preference for 7-chloro-l-tryptophan, suggesting its likely role as the natural early pathway substrate. Furthermore, the native RebO enzyme has evident, albeit limited, flexibility as shown by bioconversion studies with unnatural substrates. This work provides the first analysis of a structural enzyme involved in construction of this important class of indolocarbazole natural products.

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