Binding analysis of a psychrotrophic FKBP22 to a folding intermediate of protein using surface plasmon resonance

SIB1 FKBP22 is a homodimer, with each subunit consisting of the C‐terminal catalytic domain and N‐terminal dimerization domain. This protein exhibits peptidyl prolyl cis–trans isomerase activity for both peptide and protein substrates. However, truncation of the N‐terminal domain greatly reduces the activity only for a protein substrate. Using surface plasmon resonance, we showed that SIB1 FKBP22 loses the binding ability to a folding intermediate of protein upon truncation of the N‐terminal domain but does not lose it upon truncation of the C‐terminal domain. We propose that the binding site of SIB1 FKBP22 to a protein substrate of PPIase is located at the N‐terminal domain.

[1]  F. Schmid,et al.  Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding , 1997, The EMBO journal.

[2]  N. Cianciotto,et al.  DNA sequence of mip, a Legionella pneumophila gene associated with macrophage infectivity , 1989, Infection and immunity.

[3]  K. Young,et al.  Isolation and Amino Acid Sequence of a New 22-kDa FKBP-like Peptidyl-prolyl cis/trans-Isomerase of Escherichia coli , 1996, The Journal of Biological Chemistry.

[4]  J. Hacker,et al.  Crystal structure of Mip, a prolylisomerase from Legionella pneumophila , 2001, Nature Structural Biology.

[5]  F. Saul,et al.  Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity. , 2004, Journal of molecular biology.

[6]  Bernd Bukau,et al.  The Hsp70 and Hsp60 Chaperone Machines , 1998, Cell.

[7]  A. Plückthun,et al.  The Periplasmic Escherichia coli Peptidylprolyl cis,trans-Isomerase FkpA , 2000, The Journal of Biological Chemistry.

[8]  F. Hartl.  Molecular chaperones in cellular protein folding , 1996, Nature.

[9]  K. Kuwajima,et al.  The chaperonin GroEL does not recognize apo-α-lactalbumin in the molten globule state , 1994, Nature Structural Biology.

[10]  A. Plückthun,et al.  High enzymatic activity and chaperone function are mechanistically related features of the dimeric E. coli peptidyl-prolyl-isomerase FkpA. , 2001, Journal of molecular biology.

[11]  J. Betton,et al.  Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli , 2001, Molecular microbiology.

[12]  K. Kuwajima,et al.  The molten globule state as a clue for understanding the folding and cooperativity of globular‐protein structure , 1989, Proteins.

[13]  S. Kanaya,et al.  Possible involvement of an FKBP family member protein from a psychrotrophic bacterium Shewanella sp. SIB1 in cold-adaptation. , 2004, European journal of biochemistry.

[14]  K. Kuwajima.  The molten globule state of α‐lactalbumin , 1996, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[15]  S. Kanaya,et al.  Stabilities and activities of the N‐ and C‐domains of FKBP22 from a psychrotrophic bacterium overproduced in Escherichia coli , 2005, The FEBS journal.

[16]  K. Young,et al.  Escherichia coli and other species of the enterobacteriaceae encode a protein similar to the family of Mip-like FK506-binding proteins , 1995, Archives of Microbiology.

[17]  P. Gershon,et al.  Stable chelating linkage for reversible immobilization of oligohistidine tagged proteins in the BIAcore surface plasmon resonance detector. , 1995, Journal of immunological methods.

[18]  J. Hacker,et al.  Biochemical and Functional Analyses of the Mip Protein: Influence of the N-Terminal Half and of Peptidylprolyl Isomerase Activity on the Virulence of Legionella pneumophila , 2003, Infection and Immunity.

[19]  T. Creighton,et al.  Conformational specificity of the chaperonin GroEL for the compact folding intermediates of alpha‐lactalbumin. , 1994, The EMBO journal.