Sequence analyses reveal that a TPR-DP module, surrounded by recombinable flanking introns, could be at the origin of eukaryotic Hop and Hip TPR-DP domains and prokaryotic GerD proteins

Cell Stress and Chaperones

Volumn 14, Issue 3, 2009, Pages 281-289

  Torres, Jorge Hernández ^a   Papandreou, Nikolaos ^b   Chomilier, Jacques ^c  

^a UNIVERSIDAD INDUSTRIAL DE SANTANDER   (Colombia)

^b AGRICULTURAL UNIVERSITY OF ATHENS   (Greece)

^c UNIVERSITÉ PIERRE ET MARIE CURIE   (France)

Author keywords

Hop; Hsp organizing protein; Hsp70 interacting protein; Hydrophobic cluster analysis; Tetratricopeptide repeat; Tpr protein

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; DIPEPTIDE; HEAT SHOCK PROTEIN 70 INTERACTING PROTEIN; HEAT SHOCK PROTEIN ORGANIZING PROTEIN; MICROORGANISM PROTEIN; PROTEIN GERD; TETRATRICOPEPTIDE REPEAT PROTEIN; UNCLASSIFIED DRUG; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90;

ARTICLE; CLUSTER ANALYSIS; CONTROLLED STUDY; DNA FLANKING REGION; EUKARYOTE; GENE STRUCTURE; GENETIC RECOMBINATION; HYDROPHOBICITY; INTRON; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROKARYOTE; PROTEIN DOMAIN; PROTEIN FAMILY; SEQUENCE ANALYSIS; AMINO ACID SEQUENCE; ANIMAL; EUKARYOTIC CELL; GENETICS; HUMAN; METABOLISM; MOLECULAR EVOLUTION; MOLECULAR GENETICS; PHYSIOLOGY; PROKARYOTIC CELL; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE;

EUKARYOTA; PROKARYOTA;

AMINO ACID SEQUENCE; ANIMALS; EUKARYOTIC CELLS; EVOLUTION, MOLECULAR; HSP70 HEAT-SHOCK PROTEINS; HSP90 HEAT-SHOCK PROTEINS; HUMANS; INTRONS; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; PROKARYOTIC CELLS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ANALYSIS, PROTEIN;

EID: 66149095144     PISSN: 13558145     EISSN: 14661268     Source Type: Journal    
DOI: 10.1007/s12192-008-0083-8     Document Type: Article

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