Dataset Information

Tsga10 encodes a 65-kilodalton protein that is processed to the 27-kilodalton fibrous sheath protein.

ABSTRACT: We had previously reported the isolation of the testis-specific human gene Tsga10, which is not expressed in testes from two infertile patients. To study its role and function, we cloned the mouse homologue Mtsga10. Mtsga10 localizes to mouse chromosome 1, band B. This region is syntenic with human chromosome 2q11.2, where Tsga10 is located. We demonstrate that Mtsga10 mRNA is expressed in testis, but not in other adult tissues, and in several human fetal tissues and primary tumors. We uncovered that different species use different first exons and, consequently, different promoters. Using several antibodies, we discovered that, in mouse testis, Mtsga10 encodes a 65-kDa spermatid protein that appears to be processed to a 27-kDa protein of the fibrous sheath, a major sperm tail structure, in mature spermatozoa. Mtsga10 protein contains a putative myosin/Ezrin/radixin/moesin (ERM) domain. Transfection of fibroblasts with GFP-Mtsga10 fusion protein results in formation of short, thick filaments and deletion of the myosin/ERM domain abolished filament formation. Our results suggest the possibility that Tsga10 plays a role in the sperm tail fibrous sheath.

SUBMITTER: Modarressi MH

PROVIDER: S-EPMC3158800 | biostudies-literature | 2004 Mar

REPOSITORIES: biostudies-literature

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Tsga10 encodes a 65-kilodalton protein that is processed to the 27-kilodalton fibrous sheath protein.

Modarressi Mohammad H MH Behnam Babak B Cheng Min M Taylor Kay E KE Wolfe Jonathan J van der Hoorn Frans A FA

Biology of reproduction 20031029 3

We had previously reported the isolation of the testis-specific human gene Tsga10, which is not expressed in testes from two infertile patients. To study its role and function, we cloned the mouse homologue Mtsga10. Mtsga10 localizes to mouse chromosome 1, band B. This region is syntenic with human chromosome 2q11.2, where Tsga10 is located. We demonstrate that Mtsga10 mRNA is expressed in testis, but not in other adult tissues, and in several human fetal tissues and primary tumors. We uncovered ...[more]

PMID: 14585816

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Project description:Leptospiral protein antigens are of interest as potential virulence factors and as candidate serodiagnostic and immunoprotective reagents. We identified leptospiral protein antigens by screening a genomic expression library with serum from a rabbit hyperimmunized with formalin-killed, virulent Leptospira kirschneri serovar grippotyphosa. Genes expressing known outer membrane lipoproteins LipL32 and LipL41, the heat shock protein GroEL, and the alpha, beta, and beta' subunits of RNA polymerase were isolated from the library. In addition, a new leptospiral gene that in Escherichia coli expressed a 45-kDa antigen with an amino-terminal signal peptide followed by the spirochetal lipobox Val(-4)-Phe(-3)-Asn(-2)-Ala(-1) (downward arrow)Cys(+1) was isolated. We designated this putative lipoprotein LipL45. Immunoblot analysis of a panel of Leptospira strains probed with LipL45 antiserum demonstrated that many low-passage strains expressed LipL45. In contrast, LipL45 was not detected in high-passage, culture-attenuated strains, suggesting that LipL45 is a virulence-associated protein. In addition, all leptospiral strains tested, irrespective of culture passage, expressed a 31-kDa antigen that was recognized by LipL45 antiserum. Southern blot and peptide mapping studies indicated that this 31-kDa antigen was derived from the carboxy terminus of LipL45; therefore, it was designated P31(LipL45). Membrane fractionation studies demonstrated that P31(LipL45) is a peripheral membrane protein. Finally, we found that P31(LipL45) levels increased as Leptospira entered the stationary phase, indicating that P31(LipL45) levels were regulated. Hamsters infected with L. kirschneri formed an antibody response to LipL45, indicating that LipL45 was expressed during infection. Furthermore, the immunohistochemistry of kidneys from infected hamsters indicated that LipL45 was expressed by L. kirschneri that colonized the renal tubule. These observations suggest that expression of LipL45 responds to environmental cues, including those encountered during infection of a mammalian host.

Dataset Information

Tsga10 encodes a 65-kilodalton protein that is processed to the 27-kilodalton fibrous sheath protein.

Publications

Tsga10 encodes a 65-kilodalton protein that is processed to the 27-kilodalton fibrous sheath protein.

Similar Datasets

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