TABLE 1.

Genes up regulated during heat shocka

Oligonucleotide and functional categoryNCBI accession no.bIdentificationIncrease in expression (fold)
Heat shock response
    EH-IP0483 284.t00002 90-kDa heat shock protein7.8
    EH-IP0992 92.t00037 90-kDa heat shock protein6.2
    EH-IP0432 256.t00015 90-kDa heat shock protein2.3
    EH-IP0298 197.t00013 Hsp70 family6.1
    EH-IP0727.2 45.t00004 70-kDa heat shock protein3.9
    EH-IP0309.1 2.t00027 DnaJ4.7
    EH-IP0309.2 2.t00027 DnaJ4.7
    EH-IP0260 18.t00071 p23 cochaperone homologue2.0
    EH-IP0136 13.t00024 BAG domain3.7
    EH-IP0958 84.t00012 FKBP homologue5.8
    EH-IP0368 216.t00010 Ehssp16.3
    EH-IP1010 99.t00006 Ubiquitin-conjugating enzyme2.4
    EH-IP0753.1 49.t00025 Ubiquitin-activating enzyme1.7
    EH-IP0962 86.t00015 PCI domain, 26S proteasome2.0
    EH-IP1063 X98567 /Q27935Ubiquitin 12.1
Regulatory factors
    EH-IP0299 198.t00003 Transcription initiation factor IIIB (BRF domain)2.5
    EH-IP0677 40.t00045 Reverse transcriptase1.8
Specific genes
    EH-IP0334.2 202.t00007 20-kDa antigen-related protein8.2
    EH-IP0312 2.t00055 Cysteine protease 68.9
    EH-IP0026 10.t00046 Cysteine protease 42.1
    EH-IP0731.1 46.t00004 Cysteine desulfurase2.3
    EH-IP0731.2 46.t00004 Cysteine desulfurase2.4
    EH-IP0791 52.t00007 Lysozyme2.0
    EH-IP0144 131.t00014 Iron-sulfur flavoprotein1.7
    EH-IP0493 29.t00025 Sugar/ion transporter1.5
    EH-IP0210.2 16.t00014 Gal/GalNAc lectin Hgl-23.7
Unknown proteins
    EH-IP0556 313.t00008 Hypothetical protein/multifamily8.8
    EH-IP0377 22.t00061 Hypothetical protein1.8
  • a The Hsp90 chaperone, together with Hsp70, helps newly synthesized proteins to fold. Identified chaperone cofactors were the following: Hsp40 (DNAJ), BAG-1, and CHIP (3, 7), which interacts with the molecular chaperones Hsp70 and Hsp90 through its TPR domain, whereas its U-box domain contains the protein’s E3 ubiquitin ligase activity. A cochaperone for Hsp90 is p23, which bears an SGS domain found in eukaryotic proteins mediating ubiquitination (22). Notice that the heat shock up regulation response also included 84.t00012, a FKBP gene encoding a protein with homology to FK506-binding proteins (FKBP or immunophilin). FKBP proteins display both peptidyl-prolyl cis-trans isomerase and chaperone activity associated with Hsp90 (9). The FKBPs also specifically bind fungal macrolides such as FK506 and rapamycin, which are not yet defined to have an anti-amoeba activity. Finally, the “313.t00008” 81-amino-acid protein sequence, with no known homologies, was encountered within at least 100 other open reading frames in E. histolytica.

  • b http://www.ncbi.nlm.nih.gov/gquery/gquery.fcgi?term=ENTAMOEBA.