Amino-acid sequence homology of a polymorphic cellular protein from human lymphocytes and the chaperonins from Escherichia coli (groEL) and chloroplasts (Rubisco-binding protein).
The human p60 (Mr 60,000) is an abundant protein in the two-dimensional electrophoresis pattern of the cellular proteins of human mitogen-stimulated lymphocytes. The p60 shows as remarkable characteristic a genetic polymorphism with two different alleles. Electrotransfer of this protein from two-dimensional gels onto siliconized glass fiber sheets and subsequent amino-acid sequence analysis has revealed a striking homology to the known bacteria and plant chaperonins, the groEL and the Rubisco-subunit-binding protein. From this sequence homology we conclude that we have identified the human chaperonin homologue.
Waldinger
D
D
Institut für Anthropologie und Humangenetik der Universität München.
Eckerskorn
C
C
Lottspeich
F
F
Cleve
H
H
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics*; D001798:Blood Proteins / Q000235:genetics*; D002352:Carrier Proteins / Q000235:genetics*; D018834:Chaperonin 60; D002736:Chloroplasts / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics*; D006360:Heat-Shock Proteins / Q000235:genetics*; D006801:Humans; D008213:Lymphocyte Activation; D008214:Lymphocytes / Q000276:immunology*; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D010944:Plants / Q000235:genetics; D012689:Sequence Homology, Nucleic Acid; D013045:Species Specificity; D014908:Triticum / Q000235:genetics
D001426:Bacterial Proteins; D001798:Blood Proteins; D002352:Carrier Proteins; D018834:Chaperonin 60; D006360:Heat-Shock Proteins; D046911:Macromolecular Substances