Three-dimensional Solution Structure of an Archaeal FKBP with a Dual Function of Peptidyl Prolyl cis–trans Isomerase and Chaperone-like Activities

Suzuki, Rintaro; Nagata, Koji; Yumoto, Fumiaki; Kawakami, Masaru; Nemoto, Nobuaki; Furutani, Masahiro; Adachi, Kyoko; Maruyama, Tadashi; Tanokura, Masaru

doi:10.1016/s0022-2836(03)00379-6

Cited by 58 publications

(92 citation statements)

References 59 publications

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“…No chaperone activity has ever been reported for PIMT, and the active isoaspartate-binding site does not display any preferential affinity for hydrophobic peptides (18). One cannot, however, exclude the presence of a distinct binding site which might display chaperone properties, such as those found in protein oxidoreductases (14,34) and protein prolyl isomerases (a hypothetical chaperone activity of PIMT has not been tested in the present work) (31). However, our results strongly favor the hypothesis that the increased solubility and stability of the recombinant protein in the PIMT-overproducing strain results from a decrease in its isoaspartate content.…”

Section: Discussionmentioning

confidence: 51%

Protein Isoaspartate Methyltransferase Is a Multicopy Suppressor of Protein Aggregation in Escherichia coli

et al. 2005

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We used preS2-S-␤-galactosidase, a three-domain fusion protein that aggregates extensively at 43°C in the cytoplasm of Escherichia coli, to search for multicopy suppressors of protein aggregation and inclusion body formation and took advantage of the known differential solubility of preS2-S-␤-galactosidase at 37 and 43°C to develop a selection procedure for the gene products that would prevent its aggregation in vivo at 43°C. First, we demonstrate that the differential solubility of preS2-S-␤-galactosidase results in a lactose-positive phenotype at 37°C as opposed to a lactose-negative phenotype at 43°C. We searched for multicopy suppressors of preS2-S-␤-galactosidase aggregation by selecting pink lactose-positive colonies on a background of white lactose-negative colonies at 43°C after transformation of bacteria with an E. coli gene bank. We discovered that protein isoaspartate methyltransferase (PIMT) is a multicopy suppressor of preS2-S-␤-galactosidase aggregation at 43°C. Overexpression of PIMT reduces the amount of preS2-S-␤-galactosidase found in inclusion bodies at 43°C and increases its amount in soluble fractions. It reduces the level of isoaspartate formation in preS2-S-␤-galactosidase and increases its thermal stability in E. coli crude extracts without increasing the thermostability of a control protein, citrate synthase, in the same extracts. We could not detect any induction of the heat shock response resulting from PIMT overexpression, as judged from amounts of DnaK and GroEL, which were similar in the PIMT-overproducing and control strains. These results suggest that PIMT might be overburdened in some physiological conditions and that its overproduction may be beneficial in conditions in which protein aggregation occurs, for example, during biotechnological protein overproduction or in protein aggregation diseases.

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Section: Discussionmentioning

confidence: 51%

Protein Isoaspartate Methyltransferase Is a Multicopy Suppressor of Protein Aggregation in Escherichia coli

et al. 2005

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“…The secondary structures are arranged in the following order: ␤ 1 , ␤ 4 , ␤ 5a , ␣ 2 , ␤ 5b , ␣ 1 , ␤ 2 , ␤ 6a , ␤ 6b , and ␤ 3 . The ␤ 5 -strand of AtFKBP13 is split into two fragments, ␤ 5a and ␤ 5b , as in Methanococcus thermolithotrophicus MtFKB17 (27) and Homo sapiens HsFKB12 (28). Between ␤ 5a and ␤ 5b is the inserted ␣ 2 -helix, similar to that of MtFKB17 (27).…”

Section: Resultsmentioning

confidence: 99%

“…The ␤ 5 -strand of AtFKBP13 is split into two fragments, ␤ 5a and ␤ 5b , as in Methanococcus thermolithotrophicus MtFKB17 (27) and Homo sapiens HsFKB12 (28). Between ␤ 5a and ␤ 5b is the inserted ␣ 2 -helix, similar to that of MtFKB17 (27). The ␤ 6 -strand, which is unique to AtFKBP13, is formed by strands ␤ 6a and ␤ 6b connected by a short loop.…”

Section: Resultsmentioning

confidence: 99%

Structural analysis uncovers a role for redox in regulating FKBP13, an immunophilin of the chloroplast thylakoid lumen

Gopalan

He²,

Balmer³

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

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Change in redox status has long been known to link light to the posttranslational regulation of chloroplast enzymes. So far, studies have been conducted primarily with thioredoxin-linked members of the stroma that function in a broad array of biosynthetic and degradatory processes. Consequently, little is known about the role of redox in regulating the growing number of enzymes found to occur in the lumen, the site of oxygen evolution in thylakoid membranes. To help fill this gap, we have studied AtFKBP13, an FKBP-type immunophilin earlier shown to interact with a redoxactive protein of the lumen, and found the enzyme to contain a pair of disulfide bonds in x-ray structural studies. These disulfides, which in protein mutagenesis experiments were shown to be essential for the associated peptidyl-prolyl isomerase activity, are unique to chloroplast FKBPs and are absent in animal and yeast counterparts. Both disulfide bonds were redox-active and were reduced by thioredoxin from either chloroplast or bacterial sources in a reaction that led to loss of enzyme activity. The results suggest a previously unrecognized paradigm for redox regulation in chloroplasts in which activation by light is achieved in concert with oxygen evolution by the oxidation of sulfhydryl groups (conversion of SH to SOS). Such a mechanism, occurring in the thylakoid lumen, is in direct contrast to regulation of enzymes in the stroma, where reduction of disulfides targeted by thioredoxin (SOS converted to SH) leads to an increase in activity in the light.

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“…For example, the differential interaction of mammalian FKBP51 and FKBP52 with steroid hormone receptor complexes is mediated by their tetratricopeptide repeat domains and C-terminal divergent sequences (45). As another example, the insert-inflap (IF) domain (46) from E. coli SlyD confers chaperone activity to this FKBP enzyme and transfer of this domain to the human FKBP12 is sufficient for improved substrate affinity by the chimeric protein (47). Similar effects have been noted for the transfer of chaperone domains from non-FKBP proteins such as GroEL and SurA (48).…”

Section: Discussionmentioning

confidence: 99%

Structure and Activity of the Peptidyl-Prolyl Isomerase Domain from the Histone Chaperone Fpr4 toward Histone H3 Proline Isomerization

Monneau

Soufari

Nelson

et al. 2013

Journal of Biological Chemistry

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Background:The yeast histone chaperone Fpr4 harbors a peptidyl-prolyl isomerase domain of the FK506-binding protein (FKBP) family. Results: Catalytic efficiency toward three peptides from histone H3 relates to residues flanking the central proline. Conclusion: Substrate residues C-terminal to the proline dictate isomerase activity by Fpr4. Significance: The findings reveal new molecular details of substrate peptide recognition by the peptidyl-prolyl isomerase domain.

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Three-dimensional Solution Structure of an Archaeal FKBP with a Dual Function of Peptidyl Prolyl cis–trans Isomerase and Chaperone-like Activities

Cited by 58 publications

References 59 publications

Protein Isoaspartate Methyltransferase Is a Multicopy Suppressor of Protein Aggregation in Escherichia coli

Protein Isoaspartate Methyltransferase Is a Multicopy Suppressor of Protein Aggregation in Escherichia coli

Structural analysis uncovers a role for redox in regulating FKBP13, an immunophilin of the chloroplast thylakoid lumen

Structure and Activity of the Peptidyl-Prolyl Isomerase Domain from the Histone Chaperone Fpr4 toward Histone H3 Proline Isomerization

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