The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

PRM1  -  protamine 1

Bos taurus

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of PRM1

  • High doses of intravenous protamine cause generalized vascular permeability changes in brain and other organs, and concomitant hypoproteinemia [1].
  • Both specific and nonspecific binding of 125I-thrombin to the endothelial cell surface was partially inhibited in the presence of protamine sulfate, after the removal of cell surface heparan sulfate by the treatment of cells with crude Flavobacterium heparinum enzyme or purified heparitinase [2].
  • Complexes of enterobacterial common antigen with protamine sulfate, with methylated bovine serum albumin or with a fraction of outer membrane proteins of two different Shigella wild types proved to be highly immunogenic in rabbits upon intravenous immunization, in contrast to the enterobacterial common antigen preparations by themselves [3].
  • To elucidate the mechanism of protamine-induced hypotension, we examined the effects of protamine on catecholamine secretion in bovine adrenal medullary cells and on the serum norepinephrine in the rat [4].
  • Highly purified Sendai virus contained a protein kinase activity which atatlysed the phosphorylation of endogenous polypeptides or exogenous protamine sulphate [5].

High impact information on PRM1


Chemical compound and disease context of PRM1


Biological context of PRM1

  • The bovine genome immediately surrounding (approximately equal to 20 kilobase pairs) the protamine gene has been mapped and reveals that the sequence flanking the 5' segment of the gene is unique, while the sequence flanking the 3' segment is repetitive [9].
  • We have since utilized the BPK59 clone as a probe, to isolate both alleles of the protamine gene from a bovine genomic library constructed in Charon 28 [9].
  • Nucleotide sequence of a bovine protamine cDNA [10].
  • We have redetermined the primary sequence for bull protamine using HPLC peptide mapping and automated amino-acid sequencing techniques and report, on the basis of these findings, that the previously published amino-acid sequence for this protein is incorrect [11].
  • However, bovine P1 protamine cDNA shared greater sequence homology with mouse P1 [12].

Anatomical context of PRM1


Associations of PRM1 with chemical compounds

  • Our results show that the number of clustered arginine residues present in the DNA binding domain is the most important factor affecting the condensation and stability of the DNA-protamine complex prior to the formation of inter-protamine disulfide cross-links [16].
  • Analyses of total free sulfhydryls show that all seven of the bull protamine cysteines are cross-linked as disulfides in mature sperm [17].
  • We have identified the disulfide cross-links in bull protamine by titrating intact bull sperm with dithiothreitol (DTT) and following the modification of each cysteine residue with tritiated iodoacetate [17].
  • 0. Intra- and intermolecular disulfides were identified by correlating the reduction of specific disulfides with the dissociation of protamine from DNA in partially reduced sperm and sperm treated with N,N'-ethylenedimaleimide, a bifunctional disulfide cross-linking agent [17].
  • In the presence of polylysine or protamine, marked phosphorylation is observed [18].

Physical interactions of PRM1


Regulatory relationships of PRM1


Other interactions of PRM1

  • A second protamine variant, protamine P2, has to date been isolated only from human and murine spermatozoa where it represents the major fraction of basic nuclear protein [22].
  • The profiles of protamine inhibition of triolein-phosphatidyl-N,N-dimethyl ethanolamine (PDME) and triolein-phosphatidyl-N-monomethyl ethanolamine (PMME) emulsions were intermediate between those of PC and PE emulsions [23].
  • A second enzyme, a constitutively released PK that phosphorylates casein or phosvitin and not protamine sulfate or mixed histones, was identified and characterized [24].
  • The primary structure of mammalian protamine I can be divided into three domains, a central DNA binding domain that is arginine-rich and amino- and carboxyl-terminal domains that are rich in cysteine residues [25].
  • The purified protamine kinase exhibited about 5% activity with casein, 8% with histone H2B, and less than 0.1% with histone H1, histone H4, glycogen synthase a from rabbit skeletal muscle, ovalbumin, bovine serum albumin, and phosvitin [13].

Analytical, diagnostic and therapeutic context of PRM1


  1. Protamine-mediated transport of albumin into brain and other organs of the rat. Binding and endocytosis of protamine-albumin complex by microvascular endothelium. Pardridge, W.M., Buciak, J.L., Kang, Y.S., Boado, R.J. J. Clin. Invest. (1993) [Pubmed]
  2. Evidence that cell surface heparan sulfate is involved in the high affinity thrombin binding to cultured porcine aortic endothelial cells. Shimada, K., Ozawa, T. J. Clin. Invest. (1985) [Pubmed]
  3. Effect of proteins on the immunogenicity of enterobacterial common antigen. Kuhn, H.M., Adamus, G., Romanowska, E., Mayer, H. Infect. Immun. (1981) [Pubmed]
  4. Inhibition by protamine of catecholamine secretion and ion influxes in bovine adrenal medullary cells in culture. Minami, K., Yanagihara, N., Segawa, K., Sata, T., Tsutsui, M., Shigematsu, A., Izumi, F. J. Pharmacol. Exp. Ther. (1996) [Pubmed]
  5. The phosphorylation of sendai virus proteins by a virus particle-associated protein kinase. Lamb, R.A. J. Gen. Virol. (1975) [Pubmed]
  6. Identification in vitro of an endothelial cell surface cofactor for antithrombin III. Parallel studies with isolated perfused rat hearts and microcarrier cultures of bovine endothelium. Busch, C., Owen, W.G. J. Clin. Invest. (1982) [Pubmed]
  7. Autophosphorylation-activated protein kinase phosphorylates and inactivates protein phosphatase 2A. Guo, H., Damuni, Z. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  8. Complexes of a modified low-molecular-weight heparin with protamine are predominantly cleared by a macrophage scavenger receptor-mediated process in rats. Stehle, G., Wunder, A., Sinn, H., Schrenk, H.H., Friedrich, E.A., Dempfle, C.E., Maier-Borst, W., Heene, D.L. J. Surg. Res. (1995) [Pubmed]
  9. Bovine protamine genes contain a single intron. The structures of the two alleles. Krawetz, S.A., Connor, W., Dixon, G.H. J. Biol. Chem. (1988) [Pubmed]
  10. Nucleotide sequence of a bovine protamine cDNA. Lee, C.H., Mansouri, A., Hecht, W., Hecht, N.B., Engel, W. Biol. Chem. Hoppe-Seyler (1987) [Pubmed]
  11. A corrected primary sequence for bull protamine. Mazrimas, J.A., Corzett, M., Campos, C., Balhorn, R. Biochim. Biophys. Acta (1986) [Pubmed]
  12. Cloning of bovine P1 protamine cDNA and the evolution of vertebrate P1 protamines. Krawetz, S.A., Connor, W., Dixon, G.H. DNA (1987) [Pubmed]
  13. Purification and properties of a distinct protamine kinase from the cytosol of bovine kidney cortex. Damuni, Z., Amick, G.D., Sneed, T.R. J. Biol. Chem. (1989) [Pubmed]
  14. Insulin stimulates the activity of a protamine kinase in isolated rat hepatocytes. Reddy, S.A., Amick, G.D., Cooper, R.H., Damuni, Z. J. Biol. Chem. (1990) [Pubmed]
  15. Clathrin-coated vesicles contain two protein kinase activities. Phosphorylation of clathrin beta-light chain by casein kinase II. Bar-Zvi, D., Branton, D. J. Biol. Chem. (1986) [Pubmed]
  16. Dynamics of protamine 1 binding to single DNA molecules. Brewer, L., Corzett, M., Lau, E.Y., Balhorn, R. J. Biol. Chem. (2003) [Pubmed]
  17. Identification of bull protamine disulfides. Balhorn, R., Corzett, M., Mazrimas, J., Watkins, B. Biochemistry (1991) [Pubmed]
  18. Control of src kinase activity by activators, inhibitors, and substrate chaperones. Abdel-Ghany, M., el-Gendy, K., Zhang, S., Racker, E. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  19. The phospho-opsin phosphatase from bovine rod outer segments. An insight into the mechanism of stimulation of type-2A protein phosphatase activity by protamine. King, A.J., Andjelkovic, N., Hemmings, B.A., Akhtar, M. Eur. J. Biochem. (1994) [Pubmed]
  20. Phosphorylation and activation of protamine kinase by two forms of a myelin basic protein kinase from extracts of bovine kidney cortex. Reddy, S.A., Guo, H., Tarun, S.Z., Damuni, Z. J. Biol. Chem. (1993) [Pubmed]
  21. Protamine kinase phosphorylates eukaryotic protein synthesis initiation factor 4E. Amick, G.D., Damuni, Z. Biochem. Biophys. Res. Commun. (1992) [Pubmed]
  22. The lack of protamine 2 (P2) in boar and bull spermatozoa is due to mutations within the P2 gene. Maier, W.M., Nussbaum, G., Domenjoud, L., Klemm, U., Engel, W. Nucleic Acids Res. (1990) [Pubmed]
  23. Studies on the inhibition of pancreatic and carboxylester lipases by protamine. Tsujita, T., Matsuura, Y., Okuda, H. J. Lipid Res. (1996) [Pubmed]
  24. Release of ecto-protein kinases by the protozoan parasite Leishmania major. Sacerdoti-Sierra, N., Jaffe, C.L. J. Biol. Chem. (1997) [Pubmed]
  25. Formation of native-like mammalian sperm cell chromatin with folded bull protamine. Vilfan, I.D., Conwell, C.C., Hud, N.V. J. Biol. Chem. (2004) [Pubmed]
  26. Electrical charge and joint inflammation. Suppression of cationic aBSA-induced arthritis with a competitive polycation. van den Berg, W.B., Joosten, L.A., van de Putte, L.B., Zwarts, W.A. Am. J. Pathol. (1987) [Pubmed]
  27. Thermodynamics and kinetics of co-operative protein-nucleic acid binding. II. Studies on the binding between protamine and calf thymus DNA. Watanabe, F., Schwarz, G. J. Mol. Biol. (1983) [Pubmed]
  28. Vertebrate protamine gene evolution I. Sequence alignments and gene structure. Oliva, R., Dixon, G.H. J. Mol. Evol. (1990) [Pubmed]
WikiGenes - Universities