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TNP1  -  transition protein 1 (during histone to...

Homo sapiens

Synonyms: STP-1, Spermatid nuclear transition protein 1, TP-1
 
 
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Disease relevance of TNP1

  • This deletion reduces TNP1 expression and may cause human male infertility [1].
  • Protein classes similar to TNP1 and TNP2 that are also found in human colonic adenocarcinomas are not detectable in polyps from familial polyposis-affected patients at times when no sign of malignancy has yet appeared [2].
  • The TP1 isolate of feline sarcoma virus encodes a fgr-related oncogene lacking gamma actin sequences [3].
  • A panel of Burkitt's lymphoma cell lines and cell lines established with virus recovered from the BL cells were analyzed by Western immunoblotting and found to contain the 53-kDa TP1 product, its degradation products, or both [4].
  • METHODS: An immunohistochemical study was performed on tumors of 18 patients with HNSCC who had preoperatively been treated with TP1 in one of three dosages (0.5 mg/kg, 1.0 mg/kg, 2.0 mg/kg body weight) [5].
 

High impact information on TNP1

  • We generated mice lacking the major TP, TP1, by targeted deletion of the Tnp1 gene in mouse embryonic stem cells [6].
  • Sperm motility was reduced severely, and approximately 60% of Tnp1-null males were infertile [6].
  • Evidence for linkage was found for chromosome 2q33-35 with PCC mapping near D2S72 and TNP1 [7].
  • We have identified the predominant endogenous substrate of both Stk1 and Stp1 as a manganese-dependent inorganic pyrophosphatase (PpaC) by liquid chromatography/tandem mass spectrometry [8].
  • The DNA binding properties of TP1 and TP2 have been discussed in relation to the significance of their transient appearance during mammalian spermiogenesis [9].
 

Biological context of TNP1

 

Anatomical context of TNP1

  • Electron microscopic in situ hybridization study of simultaneous expression of TNP1 and PRM1 genes in human spermatids [12].
  • Using a series of human-rodent somatic cell hybrids containing variant complements of human chromosomes, the TNP1 gene was found to cosegregate with human chromosome 2 [13].
  • The results suggest that a labile TP1 protein may be expressed by most, if not all, EBV-infected cell lines [4].
  • The terminal protein (TP) gene produces two overlapping mRNAs in latently infected lymphocytes that are predicted to encode the similar polypeptides TP1 (497 amino acids) and TP2 (378 amino acids), with TP1 exon 1 providing 119 extra unique residues at the N terminus [4].
  • RESULTS: A highly significant, denser T-cell infiltration into the stromal tissue area of tumors of patients who had been treated with TP1 when compared with tumors of non-TP1-treated patients was observed for all three dosages [5].
 

Associations of TNP1 with chemical compounds

  • Digoxigenin or Biotin labeled probes, coding respectively for human transition protein 1 (TP1) and protamine 1 (HP1), were used for double EM in situ hybridization [12].
  • Biochemical assays revealed that Stk1 has kinase activity and localizes to the membrane and that Stp1 is a soluble protein with manganese-dependent phosphatase activity on Stk1 [8].
  • The reactions of p-nitrophenyl phosphate (pNPP) with the low-molecular mass tyrosine phosphatase Stp1 and with the mutants D128N, D128A, D128E, and S18A have been studied by measurement of heavy-atom isotope effects in the substrate [14].
  • In most individuals, TP1 treatment was associated with an improvement in cutaneous delayed-type response to PPD [15].
  • The disulfide-linked TP-1 does not cause any disorder to the neutral POPC and POPC/cholesterol membranes but induces both micellization and random orientation distribution to the anionic POPE/POPG membranes above a peptide concentration of 2% [16].
 

Other interactions of TNP1

  • We assume that the disturbances in the sperm chromatin condensation of our patients, and those described in the literature, are not primarily due to mutations in the genes for PRM1, PRM2 and TNP1 [17].
  • These spermatids were devoid of both CREM and TP1 but did contain H1t [10].
  • From this analysis we deduced that the XRCC5 gene was tightly linked to the marker, TNP1, which is located in the region 2q35 [18].
 

Analytical, diagnostic and therapeutic context of TNP1

  • In addition, one PCR primer pair was made that amplifies a restriction fragment length polymorphism on the TNP1 gene (Hoth and Engel, 1991) [19].
  • Three major derivatives, TNP-1, TNP-2, and TNP-3, were separated by high-performance liquid chromatography (HPLC) from the reaction mixtures in the absence of Ca2+ [20].
  • The results of amino acid analysis and sequence determination revealed that CDNP-PLA2 and TNP-1 contained one modified Lys residue at position 6, and both Lys-6 and Lys-62 were modified in TNP-2 [21].
  • The nucleic acid binding properties of TP2 were studied by fluorescence quenching, thermal denaturation, circular dichroism techniques and compared with those of TP1 (Singh, J., and Rao, M. R. S. (1987) J. Biol. Chem. 262, 734-740) [9].
  • Immunoprecipitation of TP products from 35S-labeled human lymphoblastoid cells (CR/B95-8) was used in pulse-chase experiments and showed that TP1 was a labile protein with a half-life of approximately 2 to 4 h [4].

References

  1. Single-nucleotide polymorphisms and mutation analyses of the TNP1 and TNP2 genes of fertile and infertile human male populations. Miyagawa, Y., Nishimura, H., Tsujimura, A., Matsuoka, Y., Matsumiya, K., Okuyama, A., Nishimune, Y., Tanaka, H. J. Androl. (2005) [Pubmed]
  2. Changes in chromosomal proteins in colon cancer: the complexity and DNA-binding properties of tumor-associated proteins and evidence for their association with the malignant state in human colonic epithelium. Boffa, L.C., Allfrey, V.G. Cancer (1977) [Pubmed]
  3. The TP1 isolate of feline sarcoma virus encodes a fgr-related oncogene lacking gamma actin sequences. Kappes, B., Ziemiecki, A., Müller, R.G., Theilen, G.H., Bauer, H., Barnekow, A. Oncogene (1989) [Pubmed]
  4. Identification of the Epstein-Barr virus terminal protein gene products in latently infected lymphocytes. Rowe, D.T., Hall, L., Joab, I., Laux, G. J. Virol. (1990) [Pubmed]
  5. Thymostimulin enhancement of T-cell infiltration into head and neck squamous cell carcinoma. Kerrebijn, J.D., Simons, P.J., Balm, A.J., Tas, M., Knegt, P.P., de Vries, N., Tan, I.B., Drexhage, H.A. Head & neck. (1996) [Pubmed]
  6. Abnormal spermatogenesis and reduced fertility in transition nuclear protein 1-deficient mice. Yu, Y.E., Zhang, Y., Unni, E., Shirley, C.R., Deng, J.M., Russell, L.D., Weil, M.M., Behringer, R.R., Meistrich, M.L. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  7. Linkage of polymorphic congenital cataract to the gamma-crystallin gene locus on human chromosome 2q33-35. Rogaev, E.I., Rogaeva, E.A., Korovaitseva, G.I., Farrer, L.A., Petrin, A.N., Keryanov, S.A., Turaeva, S., Chumakov, I., St George-Hyslop, P., Ginter, E.K. Hum. Mol. Genet. (1996) [Pubmed]
  8. A eukaryotic type serine/threonine kinase and phosphatase in Streptococcus agalactiae reversibly phosphorylate an inorganic pyrophosphatase and affect growth, cell segregation, and virulence. Rajagopal, L., Clancy, A., Rubens, C.E. J. Biol. Chem. (2003) [Pubmed]
  9. Interaction of spermatid-specific protein TP2 with nucleic acids, in vitro. A comparative study with TP1. Baskaran, R., Rao, M.R. J. Biol. Chem. (1990) [Pubmed]
  10. Round spermatids show normal testis-specific H1t but reduced cAMP-responsive element modulator and transition protein 1 expression in men with round-spermatid maturation arrest. Steger, K., Klonisch, T., Gavenis, K., Behr, R., Schaller, V., Drabent, B., Doenecke, D., Nieschlag, E., Bergmann, M., Weinbauer, G.F. J. Androl. (1999) [Pubmed]
  11. The genes for protamine 1 and 2 (PRM1 and PRM2) and transition protein 2 (TNP2) are closely linked in the mammalian genome. Engel, W., Keime, S., Kremling, H., Hameister, H., Schlüter, G. Cytogenet. Cell Genet. (1992) [Pubmed]
  12. Electron microscopic in situ hybridization study of simultaneous expression of TNP1 and PRM1 genes in human spermatids. Siffroi, J.P., Alfonsi, M.F., Dadoune, J.P. Italian journal of anatomy and embryology = Archivio italiano di anatomia ed embriologia. (1998) [Pubmed]
  13. Nucleotide sequence of the gene for human transition protein 1 and its chromosomal localization on chromosome 2. Luerssen, H., Mattei, M.G., Schröter, M., Grzeschik, K.H., Adham, I.M., Engel, W. Genomics (1990) [Pubmed]
  14. Examination of the transition state of the low-molecular mass small tyrosine phosphatase 1. Comparisons with other protein phosphatases. Hengge, A.C., Zhao, Y., Wu, L., Zhang, Z.Y. Biochemistry (1997) [Pubmed]
  15. Immune dysfunction in the elderly: effect of thymic hormone administration on several in vivo and in vitro immune function parameters. Fagiolo, U., Amadori, A., Borghesan, F., Zamarchi, R., Veronese, M.L., De Silvestro, G., Passarella, E., Crepaldi, G. Aging (Milan, Italy) (1990) [Pubmed]
  16. Peptide-lipid interactions of the beta-hairpin antimicrobial peptide tachyplesin and its linear derivatives from solid-state NMR. Doherty, T., Waring, A.J., Hong, M. Biochim. Biophys. Acta (2006) [Pubmed]
  17. Disturbances of nuclear condensation in human spermatozoa: search for mutations in the genes for protamine 1, protamine 2 and transition protein 1. Schlicker, M., Schnülle, V., Schneppel, L., Vorob'ev, V.I., Engel, W. Hum. Reprod. (1994) [Pubmed]
  18. Subchromosomal localization of a gene (XRCC5) involved in double strand break repair to the region 2q34-36. Hafezparast, M., Kaur, G.P., Zdzienicka, M., Athwal, R.S., Lehmann, A.R., Jeggo, P.A. Somat. Cell Mol. Genet. (1993) [Pubmed]
  19. Dinucleotide repeat loci contribute highly informative genetic markers to the human chromosome 2 linkage map. Todd, S., Sherman, S.L., Naylor, S.L. Genomics (1993) [Pubmed]
  20. Probing calcium ion-induced conformational changes of Taiwan cobra phospholipase A2 by trinitrophenylation of lysine residues. Chang, L.S., Lin, S.R., Chang, C.C. J. Protein Chem. (1997) [Pubmed]
  21. Functional involvement of Lys-6 in the enzymatic activity of phospholipase A2 from Bungarus multicinctus (Taiwan banded krait) snake venom. Chang, L.S., Kuo, K.W., Lin, S.R., Chang, C.C. J. Protein Chem. (1994) [Pubmed]
 
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