Global InformationParvulin 17 information
Par17, a member of the parvulin family of peptidyl-prolyl-cis/trans-isomerases (PPIases), is an isoform of parvulin 14 (Par14) and originates from alternative transcription initiation of the PIN4 gene on chromosome Xq13 in humans.[1][2] Par17, which carries a 25 residue N-terminal extension, shares the complete successive amino acid sequence with Par14. In contrast to Par14, Par17 is exclusively expressed in Hominidae, as ORFs were only found within the genomes of orangutans, gorillas, chimpanzees and humans.[3] The N-terminal extension seems to be responsible for the translocation of Par17 to the mitochondrial matrix.[3] Par17 is involved in tubulin[4][5] and actin[6] polymerization as well as in hepatitis B virus replication.[7] Using photoaffinity labeling and liquid chromatography–mass spectrometry analysis, Par17 was found to be associated with mitochondrial proteins such as members of the electron transport chain in human cells.[6]
- ^ Mueller, Jonathan; Kessler, Daniel; Neumann, Daniel; Stratmann, Tina; Papatheodorou, Panagiotis; Hartmann-Fatu, Cristina; Bayer, Peter (2006). "Characterization of novel elongated Parvulin isoforms that are ubiquitously expressed in human tissues and originate from alternative transcription initiation". BMC Molecular Biology. 7: 9. doi:10.1186/1471-2199-7-9. PMC 1420321. PMID 16522211.
- ^ Matena, Anja; Rehic, Edisa; Hönig, Dana; Kamba, Bianca; Bayer, Peter (2018). "Structure and function of the human parvulins Pin1 and Par14/17". Biological Chemistry. 399 (2): 101–125. doi:10.1515/hsz-2017-0137. PMID 29040060. S2CID 46851627.
- ^ a b Kessler, Daniel; Papatheodorou, Panagiotis; Stratmann, Tina; Dian, Elke; Hartmann-Fatu, Cristina; Rassow, Joachim; Bayer, Peter; Mueller, Jonathan (2007). "The DNA binding parvulin Par17 is targeted to the mitochondrial matrix by a recently evolved prepeptide uniquely present in Hominidae". BMC Biology. 5: 37. doi:10.1186/1741-7007-5-37. PMC 2031878. PMID 17875217.
- ^ Thiele, Alexandra; Krentzlin, Karolin; Erdmann, Frank; Rauh, David; Hause, Gerd; Zerweck, Johannes; Kilka, Susann; Pösel, Stephanie; Fischer, Gunter; Schutkowski, Mike; Weiwad, Matthias (2011). "Parvulin 17 Promotes Microtubule Assembly by Its Peptidyl-Prolyl Cis/Trans Isomerase Activity". Journal of Molecular Biology. 411 (4): 896–909. doi:10.1016/j.jmb.2011.06.040. PMID 21756916.
- ^ Burgardt, Noelia Inés; Schmidt, Andreas; Manns, Annika; Schutkowski, Alexandra; Jahreis, Günther; Lin, Yi-Jan; Schulze, Bianca; Masch, Antonia; Lücke, Christian; Weiwad, Matthias (2015). "Parvulin 17-catalyzed Tubulin Polymerization is Regulated by Calmodulin in a Calcium-dependent Manner". Journal of Biological Chemistry. 290 (27): 16708–16722. doi:10.1074/jbc.M114.593228. PMC 4505421. PMID 25940090.
- ^ a b Goehring, Anna; Michin, Irina; Gerdes, Tina; Schulze, Nina; Blueggel, Mike; Rehic, Edisa; Kaschani, Farnusch; Kaiser, Markus; Bayer, Peter (2020). "Targeting of parvulin interactors by diazirine mediated cross-linking discloses a cellular role of human Par14/17 in actin polymerization". Biological Chemistry. 401 (8): 955–968. doi:10.1515/hsz-2019-0423. PMID 32142471. S2CID 212621904.
- ^ Saeed, Umar; Kim, Jumi; Piracha, Zahra Zahid; Kwon, Hyeonjoong; Jung, Jaesung; Chwae, Yong-Joon; Park, Sun; Shin, Ho-Joon; Kim, Kyongmin (2018). "Parvulin 14 and Parvulin 17 Bind to HBX and cccDNA and Upregulate Hepatitis B Virus Replication from cccDNA to Virion in an HBX-Dependent Manner". Journal of Virology. 93 (6). doi:10.1128/JVI.01840-18. PMC 6401437. PMID 30567987.