PMID- 23345541
OWN - NLM
STAT- MEDLINE
DCOM- 20130828
LR  - 20211021
IS  - 2046-2441 (Electronic)
IS  - 2046-2441 (Linking)
VI  - 3
IP  - 1
DP  - 2013 Jan 23
TI  - Morphological development and cytochrome c oxidase activity in Streptomyces 
      lividans are dependent on the action of a copper bound Sco protein.
PG  - 120163
LID - 10.1098/rsob.120163 [doi]
LID - 120163
AB  - Copper has an important role in the life cycle of many streptomycetes, 
      stimulating the developmental switch between vegetative mycelium and aerial 
      hyphae concomitant with the production of antibiotics. In streptomycetes, a gene 
      encoding for a putative Sco-like protein has been identified and is part of an 
      operon that contains two other genes predicted to handle cellular copper. We 
      report on the Sco-like protein from Streptomyces lividans (Sco(Sl)) and present a 
      series of experiments that firmly establish a role for Sco(Sl) as a copper 
      metallochaperone as opposed to a role as a thiol-disulphide reductase that has 
      been assigned to other bacterial Sco proteins. Under low copper concentrations, a 
      Deltasco mutant in S. lividans displays two phenotypes; the development switch 
      between vegetative mycelium and aerial hyphae stalls and cytochrome c oxidase 
      (CcO) activity is significantly decreased. At elevated copper levels, the 
      development and CcO activity in the Deltasco mutant are restored to wild-type levels 
      and are thus independent of Sco(Sl). A CcO knockout reveals that morphological 
      development is independent of CcO activity leading us to suggest that Sco(Sl) has 
      at least two targets in S. lividans. We establish that one Sco(Sl) target is the 
      dinuclear Cu(A) domain of CcO and it is the cupric form of Sco(Sl) that is 
      functionally active. The mechanism of cupric ion capture by Sco(Sl) has been 
      investigated, and an important role for a conserved His residue is identified.
FAU - Blundell, Katie L I M
AU  - Blundell KL
AD  - School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 
      3SQ, UK.
FAU - Wilson, Michael T
AU  - Wilson MT
FAU - Svistunenko, Dimitri A
AU  - Svistunenko DA
FAU - Vijgenboom, Erik
AU  - Vijgenboom E
FAU - Worrall, Jonathan A R
AU  - Worrall JA
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20130123
PL  - England
TA  - Open Biol
JT  - Open biology
JID - 101580419
RN  - 0 (Bacterial Proteins)
RN  - 789U1901C5 (Copper)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
SB  - IM
MH  - Bacterial Proteins/*metabolism
MH  - Copper/*metabolism
MH  - Electron Transport Complex IV/*metabolism
MH  - Mutation
MH  - Protein Binding
MH  - Streptomyces lividans/*enzymology/genetics/*metabolism
PMC - PMC3603459
EDAT- 2013/01/25 06:00
MHDA- 2013/08/29 06:00
PMCR- 2013/01/01
CRDT- 2013/01/25 06:00
PHST- 2013/01/25 06:00 [entrez]
PHST- 2013/01/25 06:00 [pubmed]
PHST- 2013/08/29 06:00 [medline]
PHST- 2013/01/01 00:00 [pmc-release]
AID - rsob.120163 [pii]
AID - rsob120163 [pii]
AID - 10.1098/rsob.120163 [doi]
PST - epublish
SO  - Open Biol. 2013 Jan 23;3(1):120163. doi: 10.1098/rsob.120163.