ClpL is a chaperone without auxiliary factors

Caseinolytic protease L (ClpL) is a member of the heat shock protein (Hsp) 100 family, which is found mostly in Gram‐positive bacteria. Here, ClpL, a major HSP in Streptococcus pneumoniae (pneumococcus), was biochemically characterized in vitro. Recombinant ClpL shows nucleotide hydrolase, refolding...

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Bibliographic Details
Published in:The FEBS journal 2015-04, Vol.282 (8), p.1352-1367
Main Authors: Park, Sang‐Sang, Kwon, Hyog‐Young, Tran, Thao Dang‐Hien, Choi, Moo‐Hyun, Jung, Seung‐Ha, Lee, Sangho, Briles, David E, Rhee, Dong‐Kwon
Format: Article
Language:English
Subjects:
adenosine diphosphate
Adenosine Triphosphatases - metabolism
adenosine triphosphate
ATP
Bacterial Proteins - metabolism
Biochemistry
chaperone
ClpL
Gram-positive bacteria
Heat shock proteins
Hsp 100 family
Luciferases - metabolism
Malate Dehydrogenase - chemistry
Malate Dehydrogenase - metabolism
Molecular Chaperones
NTPase activity
Nucleoside-Triphosphatase - metabolism
Proteases
Protein Folding
proteinases
Streptococcus pneumoniae
Streptococcus pneumoniae - metabolism
Streptococcus pneumoniae
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Summary:Caseinolytic protease L (ClpL) is a member of the heat shock protein (Hsp) 100 family, which is found mostly in Gram‐positive bacteria. Here, ClpL, a major HSP in Streptococcus pneumoniae (pneumococcus), was biochemically characterized in vitro. Recombinant ClpL shows nucleotide hydrolase, refolding, holdase and disaggregation activity using either Mg²⁺or Mn²⁺and does not require the DnaK system for chaperone activity. ClpL exhibits two features distinct from other HSP100 family proteins: (a) Mn²⁺enhances hydrolase activity, as well as chaperone activity; and (b) NTPase activity. ClpL forms a hexamer in the presence of ADP, ATP and ATP‐γ‐S. Mutational analysis using double‐mutant proteins mutated at the two Walker A motifs (K127A/T128A and K458A/T459A) revealed that both nucleotide‐binding domains are involved in chaperone activity, ATP hydrolase activity and hexamerization. Overall, pneumococcal ClpL is a unique Mn²⁺‐dependent Hsp100 family member that has chaperone activity without other co‐chaperones.
ISSN:1742-464X
1742-4658
DOI:10.1111/febs.13228