Structural model, physiology and regulation of Slr0006 in Synechocystis PCC 6803.

D Carmel; Käthe Dahlström; M Holmström; Y Allahverdiyeva; N Battchikova; EM Aro; Tiina Salminen; P Mulo

doi:10.1007/s00203-013-0924-4

Structural model, physiology and regulation of Slr0006 in Synechocystis PCC 6803.

D Carmel, Käthe Dahlström, M Holmström, Y Allahverdiyeva, N Battchikova, EM Aro, Tiina Salminen, P Mulo

Research output: Contribution to journal › Article › Scientific › peer-review

4 Citations (Scopus)

Abstract

The slr0006 gene of Synechocystis sp. PCC 6803 is upregulated at mRNA and protein level under carbon limitation. The T(N11)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 α/β 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.

Original language	Undefined/Unknown
Pages (from-to)	727–736
Journal	Archives of Microbiology
Volume	195
Issue number	10-11
DOIs	https://doi.org/10.1007/s00203-013-0924-4
Publication status	Published - 2013
MoE publication type	A1 Journal article-refereed

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10.1007/s00203-013-0924-4

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@article{86408a455676492d89773504e8139829,

title = "Structural model, physiology and regulation of Slr0006 in Synechocystis PCC 6803.",

abstract = "The slr0006 gene of Synechocystis sp. PCC 6803 is upregulated at mRNA and protein level under carbon limitation. The T(N11)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 α/β 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.",

author = "D Carmel and K{\"a}the Dahlstr{\"o}m and M Holmstr{\"o}m and Y Allahverdiyeva and N Battchikova and EM Aro and Tiina Salminen and P Mulo",

year = "2013",

doi = "10.1007/s00203-013-0924-4",

language = "Odefinierat/ok{\"a}nt",

volume = "195",

pages = "727–736",

journal = "Archives of Microbiology",

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TY - JOUR

T1 - Structural model, physiology and regulation of Slr0006 in Synechocystis PCC 6803.

AU - Carmel, D

AU - Dahlström, Käthe

AU - Holmström, M

AU - Allahverdiyeva, Y

AU - Battchikova, N

AU - Aro, EM

AU - Salminen, Tiina

AU - Mulo, P

PY - 2013

Y1 - 2013

N2 - The slr0006 gene of Synechocystis sp. PCC 6803 is upregulated at mRNA and protein level under carbon limitation. The T(N11)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 α/β 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.

AB - The slr0006 gene of Synechocystis sp. PCC 6803 is upregulated at mRNA and protein level under carbon limitation. The T(N11)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 α/β 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.

U2 - 10.1007/s00203-013-0924-4

DO - 10.1007/s00203-013-0924-4

M3 - Artikel

SN - 0302-8933

VL - 195

SP - 727

EP - 736

JO - Archives of Microbiology

JF - Archives of Microbiology

IS - 10-11

ER -