ClpL is a functionally active tetradecameric AAA+ chaperone, distinct from hexameric/dodecameric ones.

Kim, Gyuhee; Lee, Seong-Gyu; Han, Seungsu; Jung, Jaeeun; Jeong, Hyeong Seop; Hyun, Jae-Kyung; Rhee, Dong-Kwon; Kim, Ho Min; Lee, Sangho

Kim, Gyuhee; Lee, Seong-Gyu; Han, Seungsu; Jung, Jaeeun; Jeong, Hyeong Seop; Hyun, Jae-Kyung; Rhee, Dong-Kwon; Kim, Ho Min; Lee, Sangho.

Afiliação

Kim G; Department of Biological Sciences, Sungkyunkwan University, Suwon, Korea.
Lee SG; Center for Biomolecular and Cellular Structure, Institute for Basic Science (IBS), Daejeon, Korea.
Han S; Graduate School of Medical Science and Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, Korea.
Jung J; Department of Biological Sciences, Sungkyunkwan University, Suwon, Korea.
Jeong HS; Department of Biological Sciences, Sungkyunkwan University, Suwon, Korea.
Hyun JK; Korea Basic Science Institute, Cheongju, Korea.
Rhee DK; Korea Basic Science Institute, Cheongju, Korea.
Kim HM; Okinawa Institute of Science and Technology Graduate University, Okinawa, Japan.
Lee S; School of Pharmacy, Sungkyunkwan University, Suwon, Korea.

FASEB J ; 34(11): 14353-14370, 2020 11.

Article em En | MEDLINE | ID: mdl-32910525

Assuntos

Proteínas de Bactérias/química; Chaperonas Moleculares/química; Multimerização Proteica; Substituição de Aminoácidos; Proteínas de Bactérias/genética; Proteínas de Bactérias/metabolismo; Chaperonas Moleculares/genética; Chaperonas Moleculares/metabolismo; Domínios Proteicos; Streptococcus pneumoniae/metabolismo

Palavras-chave

S. pneumoniae; ClpL; Hsp100; chaperone; tetradecamer

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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Bactérias / Chaperonas Moleculares / Multimerização Proteica Idioma: En Ano de publicação: 2020 Tipo de documento: Article

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