Structural Adaptations in the Specialized Bacteriophage T4 Co-Chaperonin Gp31 Expand the Size of the Anfinsen Cage

Hunt, J.F.; Vies, Saskia M. van der; Henry, Lisa; Deisenhofer, Johann

doi:10.1016/s0092-8674(00)80343-8

Cited by 97 publications

(83 citation statements)

References 64 publications

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“…Because T4 cannot propagate in the absence of Gp31, GroES cannot substitute for Gp31 (21). From its crystal structure, the roof structure of Gp31 was found to be completely absent, leaving a cavity of at least 16 Å in diameter (26). Due to the absence of the roof structure of Gp31, the complexes between GroEL and Gp31 might have a larger substrate-binding cavity than GroEL and GroES.…”

Section: Resultsmentioning

confidence: 99%

Chloroplasts Have a Novel Cpn10 in Addition to Cpn20 as Co-chaperonins in Arabidopsis thaliana

Koumoto¹,

Shimada²,

Kondo³

et al. 2001

Journal of Biological Chemistry

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Previously, we characterized a mitochondrial co-chaperonin (Cpn10) and a chloroplast co-chaperonin (Cpn20) from Arabidopsis thaliana (Koumoto, Y., Tsugeki, R., Shimada, T., Mori, H., Kondo, M., Hara-Nishimura, I., and Nishimura, M. (1996) Plant J. 10, 1119-1125; Koumoto, Y., Shimada, T., Kondo, M., Takao, T., Shimonishi, Y., HaraNishimura, I., and Nishimura, M. (1999) Plant J. 17, 467-477). Here, we report a third co-chaperonin. The cDNA was 603 base pairs long, encoding a protein of 139 amino acids. From a sequence analysis, the protein was predicted to have one Cpn10 domain with an amino-terminal extension that might work as a chloroplast transit peptide. This novel Cpn10 was confirmed to be localized in chloroplasts, and we refer to it as chloroplast Cpn10 (chl-Cpn10). The phylogenic tree that was generated with amino acid sequences of other co-chaperonins indicates that chl-Cpn10 is highly divergent from the others. In the GroEL-assisted protein folding assay, about 30% of the substrates were refolded with chl-Cpn10, indicating that chl-Cpn10 works as a cochaperonin. A Northern blot analysis revealed that mRNA for chl-Cpn10 is accumulated in the leaves and stems, but not in the roots. In germinating cotyledons, the accumulation of chl-Cpn10 was similar to that of chloroplastic proteins and accelerated by light. It was proposed that two kinds of co-chaperonins, Cpn20 and chl-Cpn10, work independently in the chloroplast.

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Section: Resultsmentioning

confidence: 99%

Chloroplasts Have a Novel Cpn10 in Addition to Cpn20 as Co-chaperonins in Arabidopsis thaliana

Koumoto¹,

Shimada²,

Kondo³

et al. 2001

Journal of Biological Chemistry

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“…Compared with GroES, the gp31 monomer has a 12-residue insertion starting at position 82, a longer mobile loop (22 vs. 16 aa), no roof ␤-hairpin, and no tyrosine at position 71, a residue that is present in all GroES-like cochaperonins and protrudes into the GroEL-GroES folding cavity. These differences, either by themselves or in combination, have been postulated to lead to a slight expansion of the GroEL-gp31 folding cage relative to the GroEL-GroES cavity (22). Preliminary cryo-electron microscopic images of the GroEL(ADP)-gp31 complex show that gp31 protrudes less far into the cavity than GroES when compared with the GroEL(ADP)-GroES crystal structure (D. K. Clare, P.J.B., H.H., S.M.V., and H. R. Saibil, unpublished results), suggestive of a larger folding cavity.…”

Section: Discussionmentioning

confidence: 99%

The T4-encoded cochaperonin, gp31, has unique properties that explain its requirement for the folding of the T4 major capsid protein

Bakkes

Faber

Heerikhuizen

et al. 2005

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

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The morphogenesis of bacteriophage T4 requires a specialized bacteriophage-encoded molecular chaperone (gp31) that is essential for the folding of the T4 major capsid protein (gp23). gp31 is related to GroES, the chaperonin of the Escherichia coli host because it displays a similar overall structure and properties. Why GroES is unable to fold the T4 capsid protein in conjunction with GroEL is unknown. Here we show that gp23 binds to the GroEL heptameric ring opposite to the ring that is bound by gp31 (the so-called trans-ring), while no binding to the trans-ring of the GroEL-GroES complex is observed. Although gp23 can be enclosed within the folding cage of the GroEL-gp31 complex, encapsulation within the GroEL-GroES complex is not possible. So it appears that folding of the T4 major capsid protein requires a gp31-dependent cis-folding mechanism likely inside an enlarged ''Anfinsen cage'' provided by GroEL and gp31.chaperones ͉ protein folding ͉ viral capsid assembly

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“…For example, although T4 bacteriophage utilizes the host chaperonin, it encodes its own version of cochaperonin, known as gp31. The recent crystal structure of gp31 (78) suggests that it can form a larger folding cavity in the cis complex (Anfinsen cage) to accommodate the >50 kDa phage head protein (gp23), which may not fit comfortably under GroES.…”

Section: The Asymmetrical Groel-groes-adp Complex Structurementioning

confidence: 99%

STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING

Sigler

Rye

et al. 1998

Annu. Rev. Biochem.

536

387

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Recent structural and biochemical investigations have come together to allow a better understanding of the mechanism of chaperonin (GroEL, Hsp60)-mediated protein folding, the final step in the accurate expression of genetic information. Major, asymmetric conformational changes in the GroEL double toroid accompany binding of ATP and the cochaperonin GroES. When a nonnative polypeptide, bound to one of the GroEL rings, is encapsulated by GroES to form a cis ternary complex, these changes drive the polypeptide into the sequestered cavity and initiate its folding. ATP hydrolysis in the cis ring primes release of the products, and ATP binding in the trans ring then disrupts the cis complex. This process allows the polypeptide to achieve its final native state, if folding was completed, or to recycle to another chaperonin molecule, if the folding process did not result in a form committed to the native state. CONTENTS

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Structural Adaptations in the Specialized Bacteriophage T4 Co-Chaperonin Gp31 Expand the Size of the Anfinsen Cage

Cited by 97 publications

References 64 publications

Chloroplasts Have a Novel Cpn10 in Addition to Cpn20 as Co-chaperonins in Arabidopsis thaliana

Chloroplasts Have a Novel Cpn10 in Addition to Cpn20 as Co-chaperonins in Arabidopsis thaliana

The T4-encoded cochaperonin, gp31, has unique properties that explain its requirement for the folding of the T4 major capsid protein

STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING

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