Folding of Aplysia limacina apomyoglobin involves an intermediate in common with other evolutionarily distant globins

In the globin family, similarities in the folding mechanism have been found among different mammalian apomyoglobins (apoMb). The best-characterized intermediate of sperm whale apoMb, called I-AGH, is mainly stabilized by nativelike contacts among the A, G, and H helices involving a cluster of hydrop...

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Published in:Biochemistry
Main Authors: MUSTO R., BIGOTTI, Maria Giulia, TRAVAGLINI ALLOCATELLI, Carlo, BRUNORI, Maurizio, CUTRUZZOLA', Francesca
Other Authors: Musto, R., Bigotti, Maria Giulia, Brunori, Maurizio, Cutruzzola', Francesca
Format: Article in Journal/Newspaper
Language:English
Published: American Chemical Society:1155 Sixteenth Street Northwest:Washington, DC 20036:(800)227-5558, EMAIL: service@acs.org, INTERNET: http://www.pubs.acs.org, Fax: (614)447-3671 2004
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Online Access:http://hdl.handle.net/11573/42406
https://doi.org/10.1021/bi035319l
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spelling ftunivromairis:oai:iris.uniroma1.it:11573/42406 2024-02-27T08:45:41+00:00 Folding of Aplysia limacina apomyoglobin involves an intermediate in common with other evolutionarily distant globins MUSTO R. BIGOTTI, Maria Giulia TRAVAGLINI ALLOCATELLI, Carlo BRUNORI, Maurizio CUTRUZZOLA', Francesca Musto, R. Bigotti, Maria Giulia TRAVAGLINI ALLOCATELLI, Carlo Brunori, Maurizio Cutruzzola', Francesca 2004 http://hdl.handle.net/11573/42406 https://doi.org/10.1021/bi035319l http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=000187894800026&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=0c7ff228ccbaaa74236f48834a34396a http://www.scopus.com/inward/record.url?eid=2-s2.0-0346096857&partnerID=65&md5=1cf32405973438d0e3733a1cee02aa4b eng eng American Chemical Society:1155 Sixteenth Street Northwest:Washington, DC 20036:(800)227-5558, EMAIL: service@acs.org, INTERNET: http://www.pubs.acs.org, Fax: (614)447-3671 info:eu-repo/semantics/altIdentifier/pmid/14705950 info:eu-repo/semantics/altIdentifier/wos/WOS:000187894800026 volume:43 firstpage:230 lastpage:236 numberofpages:7 journal:BIOCHEMISTRY http://hdl.handle.net/11573/42406 doi:10.1021/bi035319l info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-0346096857 http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=000187894800026&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=0c7ff228ccbaaa74236f48834a34396a http://www.scopus.com/inward/record.url?eid=2-s2.0-0346096857&partnerID=65&md5=1cf32405973438d0e3733a1cee02aa4b MOLTEN GLOBULE INTERMEDIATE PROTEIN STABILITY MYOGLOBIN PROTEIN DENATURATION REACTION KINETICS info:eu-repo/semantics/article 2004 ftunivromairis https://doi.org/10.1021/bi035319l 2024-01-31T17:44:25Z In the globin family, similarities in the folding mechanism have been found among different mammalian apomyoglobins (apoMb). The best-characterized intermediate of sperm whale apoMb, called I-AGH, is mainly stabilized by nativelike contacts among the A, G, and H helices involving a cluster of hydrophobic residues that includes two conserved tryptophans. To verify the hypothesis of a common intermediate in the folding of all members of the globin family, we have extensively studied a sitedirected mutant of the myoglobin from Aplysia limacina, distantly related to the mammalian counterpart, in which one of the two tryptophans in the A-G-H cluster [i.e., Trp(H8)130] has been mutated to tyrosine. The results presented here show that this mutation destabilizes both the native state and the acid intermediate IA but exerts little or no effect on the thermally stable core of an intermediate species (called IT) peculiar to Aplysia apomyoglobin. Dynamic quenching of Trp emission by acrylamide provides information on the accessibility of the chromophores at the native and the intermediate states of wild-type and mutant Aplysia apomyoglobin, consistent with the thermodynamics. Our results agree well with those obtained for the corresponding topological position of apomyoglobin from sperm whale and clearly show that the H8 position is involved in the stabilization of the main intermediate in both apoproteins. This residue thus plays a role which is evolutionarily conserved in the globin family from invertebrates to mammals; our results support the contention that the A-G-H cluster is important in the folding pathway of different globins. Article in Journal/Newspaper Sperm whale Sapienza Università di Roma: CINECA IRIS Biochemistry 43 1 230 236
institution Open Polar
collection Sapienza Università di Roma: CINECA IRIS
op_collection_id ftunivromairis
language English
topic MOLTEN GLOBULE INTERMEDIATE
PROTEIN STABILITY
MYOGLOBIN
PROTEIN DENATURATION
REACTION KINETICS
spellingShingle MOLTEN GLOBULE INTERMEDIATE
PROTEIN STABILITY
MYOGLOBIN
PROTEIN DENATURATION
REACTION KINETICS
MUSTO R.
BIGOTTI, Maria Giulia
TRAVAGLINI ALLOCATELLI, Carlo
BRUNORI, Maurizio
CUTRUZZOLA', Francesca
Folding of Aplysia limacina apomyoglobin involves an intermediate in common with other evolutionarily distant globins
topic_facet MOLTEN GLOBULE INTERMEDIATE
PROTEIN STABILITY
MYOGLOBIN
PROTEIN DENATURATION
REACTION KINETICS
description In the globin family, similarities in the folding mechanism have been found among different mammalian apomyoglobins (apoMb). The best-characterized intermediate of sperm whale apoMb, called I-AGH, is mainly stabilized by nativelike contacts among the A, G, and H helices involving a cluster of hydrophobic residues that includes two conserved tryptophans. To verify the hypothesis of a common intermediate in the folding of all members of the globin family, we have extensively studied a sitedirected mutant of the myoglobin from Aplysia limacina, distantly related to the mammalian counterpart, in which one of the two tryptophans in the A-G-H cluster [i.e., Trp(H8)130] has been mutated to tyrosine. The results presented here show that this mutation destabilizes both the native state and the acid intermediate IA but exerts little or no effect on the thermally stable core of an intermediate species (called IT) peculiar to Aplysia apomyoglobin. Dynamic quenching of Trp emission by acrylamide provides information on the accessibility of the chromophores at the native and the intermediate states of wild-type and mutant Aplysia apomyoglobin, consistent with the thermodynamics. Our results agree well with those obtained for the corresponding topological position of apomyoglobin from sperm whale and clearly show that the H8 position is involved in the stabilization of the main intermediate in both apoproteins. This residue thus plays a role which is evolutionarily conserved in the globin family from invertebrates to mammals; our results support the contention that the A-G-H cluster is important in the folding pathway of different globins.
author2 Musto, R.
Bigotti, Maria Giulia
TRAVAGLINI ALLOCATELLI, Carlo
Brunori, Maurizio
Cutruzzola', Francesca
format Article in Journal/Newspaper
author MUSTO R.
BIGOTTI, Maria Giulia
TRAVAGLINI ALLOCATELLI, Carlo
BRUNORI, Maurizio
CUTRUZZOLA', Francesca
author_facet MUSTO R.
BIGOTTI, Maria Giulia
TRAVAGLINI ALLOCATELLI, Carlo
BRUNORI, Maurizio
CUTRUZZOLA', Francesca
author_sort MUSTO R.
title Folding of Aplysia limacina apomyoglobin involves an intermediate in common with other evolutionarily distant globins
title_short Folding of Aplysia limacina apomyoglobin involves an intermediate in common with other evolutionarily distant globins
title_full Folding of Aplysia limacina apomyoglobin involves an intermediate in common with other evolutionarily distant globins
title_fullStr Folding of Aplysia limacina apomyoglobin involves an intermediate in common with other evolutionarily distant globins
title_full_unstemmed Folding of Aplysia limacina apomyoglobin involves an intermediate in common with other evolutionarily distant globins
title_sort folding of aplysia limacina apomyoglobin involves an intermediate in common with other evolutionarily distant globins
publisher American Chemical Society:1155 Sixteenth Street Northwest:Washington, DC 20036:(800)227-5558, EMAIL: service@acs.org, INTERNET: http://www.pubs.acs.org, Fax: (614)447-3671
publishDate 2004
url http://hdl.handle.net/11573/42406
https://doi.org/10.1021/bi035319l
http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=000187894800026&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=0c7ff228ccbaaa74236f48834a34396a
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genre Sperm whale
genre_facet Sperm whale
op_relation info:eu-repo/semantics/altIdentifier/pmid/14705950
info:eu-repo/semantics/altIdentifier/wos/WOS:000187894800026
volume:43
firstpage:230
lastpage:236
numberofpages:7
journal:BIOCHEMISTRY
http://hdl.handle.net/11573/42406
doi:10.1021/bi035319l
info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-0346096857
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container_title Biochemistry
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