A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Structural model, physiology and regulation of Slr0006 in Synechocystis PCC 6803
Tekijät: Carmel D, Dahlström KM, Holmström M, Allahverdiyeva Y, Battchikova N, Aro EM, Salminen TA, Mulo P
Kustantaja: SPRINGER
Julkaisuvuosi: 2013
Journal: Archives of Microbiology
Tietokannassa oleva lehden nimi: ARCHIVES OF MICROBIOLOGY
Lehden akronyymi: ARCH MICROBIOL
Numero sarjassa: 10-11
Vuosikerta: 195
Numero: 10-11
Aloitussivu: 727
Lopetussivu: 736
Sivujen määrä: 10
ISSN: 0302-8933
DOI: https://doi.org/10.1007/s00203-013-0924-4
Tiivistelmä
The slr0006 gene of Synechocystis sp. PCC 6803 is upregulated at mRNA and protein level under carbon limitation. The T(N-11)A motif in the upstream region of slr0006 is a binding site for transcriptional regulator NdhR, and accumulation of the Slr0006 protein in ndhR deletion mutant grown in high CO2 suggests that NdhR may be a negative regulator of slr0006. Accumulation requires photosynthetic electron transfer, because no Slr0006 was detected in darkness or in the presence of electron transfer inhibitors DCMU and DBMIB. Structural modeling of the Slr0006 protein suggests that it adopts Sua5/YciO/YrdC family fold, which is an alpha/beta twisted open-sheet structure. Similar to the structurally known members of this protein family, the surface of Slr0006 contains positively charged cavity indicating a possible binding site for RNA or nucleotides. Moreover, Slr0006 was co-localized with 30S ribosomal proteins and rRNA, suggesting involvement in processes linked to protein synthesis.
The slr0006 gene of Synechocystis sp. PCC 6803 is upregulated at mRNA and protein level under carbon limitation. The T(N-11)A motif in the upstream region of slr0006 is a binding site for transcriptional regulator NdhR, and accumulation of the Slr0006 protein in ndhR deletion mutant grown in high CO2 suggests that NdhR may be a negative regulator of slr0006. Accumulation requires photosynthetic electron transfer, because no Slr0006 was detected in darkness or in the presence of electron transfer inhibitors DCMU and DBMIB. Structural modeling of the Slr0006 protein suggests that it adopts Sua5/YciO/YrdC family fold, which is an alpha/beta twisted open-sheet structure. Similar to the structurally known members of this protein family, the surface of Slr0006 contains positively charged cavity indicating a possible binding site for RNA or nucleotides. Moreover, Slr0006 was co-localized with 30S ribosomal proteins and rRNA, suggesting involvement in processes linked to protein synthesis.
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