抄録
Streptococcus intermedius DnaK complements the temperature-sensitive phenotype of an Escherichia coli dnaK null mutant only when co-chaperones DnaJ and GrpE are co-expressed. Therefore, whether S. intermedius DnaK and E. coli DnaK can recognize heterologous co-chaperones in vitro was examined. Addition of heterologous GrpE to DnaK and DnaJ partially stimulated adenosine triphosphatase (ATPase) activity, and almost completely stimulated luciferase refolding activity. Addition of heterologous DnaJ to GrpE and DnaK also stimulated ATPase activity; however, significant luciferase refolding activity was not observed. Moreover, E. coli DnaJ had a negative effect on the luciferase refolding activity of the S. intermedius DnaK chaperone system. In E. coli chaperone mutants, with the exception of E. coli DnaJ, stronger expression of the heterologous co-chaperones partially or almost completely complemented the temperature-sensitive-phenotype. These results indicate that all heterologous co-chaperones can at least partially recognize DnaK of a distantly related species. A region of the ATPase domain that is present in the DnaK of gram-negative bacteria is absent from the DnaK of gram-positive bacteria. This region is believed to be important for recognition of co-chaperones from gram-negative bacteria. However, insertion of this segment into S. intermedius DnaK failed to increase its ability to recognize E. coli co-chaperones, implying that this region is unnecessary or insufficient for the recognition of E. coli co-chaperones. Thus, our data suggest that a basic structural similarity is conserved among the components of the S. intermedius and E. coli DnaK chaperone systems, allowing weak associations between heterologous components.
| 元の言語 | 英語 |
|---|---|
| ページ（範囲） | 681-693 |
| ページ数 | 13 |
| ジャーナル | MICROBIOLOGY and IMMUNOLOGY |
| 巻 | 62 |
| 発行部数 | 11 |
| DOI | |
| 出版物ステータス | 出版済み - 11 1 2018 |
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All Science Journal Classification (ASJC) codes
- Microbiology
- Immunology
- Virology
これを引用
Recognizability of heterologous co-chaperones with Streptococcus intermedius DnaK and Escherichia coli DnaK. / Tomoyasu, Toshifumi; Tsuruno, Keigo; Tanatsugu, Ryosuke; Miyazaki, Aya; Kondo, Hiroyuki; Tabata, Atsushi; Whiley, Robert A.; Sonomoto, Kenji; Nagamune, Hideaki.
：: MICROBIOLOGY and IMMUNOLOGY, 巻 62, 番号 11, 01.11.2018, p. 681-693.研究成果: ジャーナルへの寄稿 › 記事
}
TY - JOUR
T1 - Recognizability of heterologous co-chaperones with Streptococcus intermedius DnaK and Escherichia coli DnaK
AU - Tomoyasu, Toshifumi
AU - Tsuruno, Keigo
AU - Tanatsugu, Ryosuke
AU - Miyazaki, Aya
AU - Kondo, Hiroyuki
AU - Tabata, Atsushi
AU - Whiley, Robert A.
AU - Sonomoto, Kenji
AU - Nagamune, Hideaki
PY - 2018/11/1
Y1 - 2018/11/1
N2 - Streptococcus intermedius DnaK complements the temperature-sensitive phenotype of an Escherichia coli dnaK null mutant only when co-chaperones DnaJ and GrpE are co-expressed. Therefore, whether S. intermedius DnaK and E. coli DnaK can recognize heterologous co-chaperones in vitro was examined. Addition of heterologous GrpE to DnaK and DnaJ partially stimulated adenosine triphosphatase (ATPase) activity, and almost completely stimulated luciferase refolding activity. Addition of heterologous DnaJ to GrpE and DnaK also stimulated ATPase activity; however, significant luciferase refolding activity was not observed. Moreover, E. coli DnaJ had a negative effect on the luciferase refolding activity of the S. intermedius DnaK chaperone system. In E. coli chaperone mutants, with the exception of E. coli DnaJ, stronger expression of the heterologous co-chaperones partially or almost completely complemented the temperature-sensitive-phenotype. These results indicate that all heterologous co-chaperones can at least partially recognize DnaK of a distantly related species. A region of the ATPase domain that is present in the DnaK of gram-negative bacteria is absent from the DnaK of gram-positive bacteria. This region is believed to be important for recognition of co-chaperones from gram-negative bacteria. However, insertion of this segment into S. intermedius DnaK failed to increase its ability to recognize E. coli co-chaperones, implying that this region is unnecessary or insufficient for the recognition of E. coli co-chaperones. Thus, our data suggest that a basic structural similarity is conserved among the components of the S. intermedius and E. coli DnaK chaperone systems, allowing weak associations between heterologous components.
AB - Streptococcus intermedius DnaK complements the temperature-sensitive phenotype of an Escherichia coli dnaK null mutant only when co-chaperones DnaJ and GrpE are co-expressed. Therefore, whether S. intermedius DnaK and E. coli DnaK can recognize heterologous co-chaperones in vitro was examined. Addition of heterologous GrpE to DnaK and DnaJ partially stimulated adenosine triphosphatase (ATPase) activity, and almost completely stimulated luciferase refolding activity. Addition of heterologous DnaJ to GrpE and DnaK also stimulated ATPase activity; however, significant luciferase refolding activity was not observed. Moreover, E. coli DnaJ had a negative effect on the luciferase refolding activity of the S. intermedius DnaK chaperone system. In E. coli chaperone mutants, with the exception of E. coli DnaJ, stronger expression of the heterologous co-chaperones partially or almost completely complemented the temperature-sensitive-phenotype. These results indicate that all heterologous co-chaperones can at least partially recognize DnaK of a distantly related species. A region of the ATPase domain that is present in the DnaK of gram-negative bacteria is absent from the DnaK of gram-positive bacteria. This region is believed to be important for recognition of co-chaperones from gram-negative bacteria. However, insertion of this segment into S. intermedius DnaK failed to increase its ability to recognize E. coli co-chaperones, implying that this region is unnecessary or insufficient for the recognition of E. coli co-chaperones. Thus, our data suggest that a basic structural similarity is conserved among the components of the S. intermedius and E. coli DnaK chaperone systems, allowing weak associations between heterologous components.
UR - http://www.scopus.com/inward/record.url?scp=85056121796&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85056121796&partnerID=8YFLogxK
U2 - 10.1111/1348-0421.12651
DO - 10.1111/1348-0421.12651
M3 - Article
C2 - 30239035
AN - SCOPUS:85056121796
VL - 62
SP - 681
EP - 693
JO - Microbiology and Immunology
JF - Microbiology and Immunology
SN - 0385-5600
IS - 11
ER -