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

Carmel, Dalton; Dahlström, Käthe; Holmström, Maija; Allahverdiyeva, Yagut; Battchikova, Natalia; Aro, Eva-Mari; Salminen, Tiina; Mulo, Paula
November 2013
Archives of Microbiology;Nov2013, Vol. 195 Issue 10/11, p727
Academic Journal
The slr0006 gene of Synechocystis sp. PCC 6803 is upregulated at mRNA and protein level under carbon limitation. The T(N)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 CO 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.


Related Articles

  • Translating the effects of mTOR on secretory senescence. Tomimatsu, Kosuke; Narita, Masashi // Nature Cell Biology;Oct2015, Vol. 17 Issue 10, p1230 

    Cellular senescence is often accompanied by the production of secreted proteins that mediate the diverse effects of senescence on the tissue microenvironment. The mammalian target of rapamycin (mTOR), a master regulator of protein synthesis, is now shown to control the senescence-associated...

  • In vivo SELEX reveals novel sequence and structural determinants of Nrd1-Nab3-Sen1-dependent transcription termination. Porrua, Odil; Hobor, Fruzsina; Boulay, Jocelyne; Kubicek, Karel; D'Aubenton-Carafa, Yves; Gudipati, Rajani Kanth; Stefl, Richard; Libri, Domenico // EMBO Journal;10/3/2012, Vol. 31 Issue 19, p3935 

    The Nrd1-Nab3-Sen1 (NNS) complex pathway is responsible for transcription termination of cryptic unstable transcripts and sn/snoRNAs. The NNS complex recognizes short motifs on the nascent RNA, but the presence of these sequences alone is not sufficient to define a functional terminator. We...

  • Genetic manipulation of a transcription-regulating sequence of porcine reproductive and respiratory syndrome virus reveals key nucleotides determining its activity. Zheng, Haihong; Zhang, Keyu; Zhu, Xing-Quan; Liu, Changlong; Lu, Jiaqi; Gao, Fei; Zhou, Yan; Zheng, Hao; Lin, Tao; Li, Liwei; Tong, Guangzhi; Wei, Zuzhang; Yuan, Shishan // Archives of Virology;Aug2014, Vol. 159 Issue 8, p1927 

    The factors that determine the transcription-regulating sequence (TRS) activity of porcine reproductive and respiratory syndrome virus (PRRSV) remain largely unclear. In this study, the effect of mutagenesis of conserved C nucleotides at positions 5 and 6 in the leader TRS (TRS-L) and/or...

  • Improving the prediction of mRNA extremities in the parasitic protozoan Leishmania. Smith, Martin; Blanchette, Mathieu; Papadopoulou, Barbara // BMC Bioinformatics;2008, Vol. 9, Special section p1 

    Background: Leishmania and other members of the Trypanosomatidae family diverged early on in eukaryotic evolution and consequently display unique cellular properties. Their apparent lack of transcriptional regulation is compensated by complex post-transcriptional control mechanisms, including...

  • hiCLIP reveals the in vivo atlas of mRNA secondary structures recognized by Staufen 1. Sugimoto, Yoichiro; Vigilante, Alessandra; Darbo, Elodie; Zirra, Alexandra; Militti, Cristina; D'Ambrogio, Andrea; Luscombe, Nicholas M.; Ule, Jernej // Nature;3/26/2015, Vol. 519 Issue 7544, p491 

    The structure of messenger RNA is important for post-transcriptional regulation, mainly because it affects binding of trans-acting factors. However, little is known about the in vivo structure of full-length mRNAs. Here we present hiCLIP, a biochemical technique for transcriptome-wide...

  • Polyamine stimulation of eEF1A synthesis based on the unusual position of a complementary sequence to 18S rRNA in eEF1A mRNA. Terui, Yusuke; Sakamoto, Akihiko; Yoshida, Taketo; Kasahara, Takuma; Tomitori, Hideyuki; Higashi, Kyohei; Igarashi, Kazuei; Kashiwagi, Keiko // Amino Acids;Feb2015, Vol. 47 Issue 2, p345 

    It is thought that Shine-Dalgarno-like sequences, which exhibit complementarity to the nucleotide sequences at the 3′-end of 18S rRNA, are not present in eukaryotic mRNAs. However, complementary sequences consisting of more than 5 nucleotides to the 3′-end of 18S rRNA, i.e., a CR...

  • Chemical Biology: Ignore the nonsense. Schmitz, Anton; Famulok, Michael // Nature;5/3/2007, Vol. 447 Issue 7140, p42 

    The article discusses the development of inherited diseases which are caused by mutations in nucleotides within genes. According to the author, these mutations can transform the products of messenger ribonucleic acid (mRNA) codon into the growing protein chain. He adds that these cellular...

  • The transorientation hypothesis for codon recognition during protein synthesis. Simonson, Anne B.; Lake, James A. // Nature;3/21/2002, Vol. 416 Issue 6878, p281 

    Examines the transorientation hypothesis for codon of messenger RNA during protein synthesis. Rotation of transfer RNA binding site; Formation of ribosomal protein L11; Interaction between initiator and methionine elongator anti-codon loop structures.

  • Structure of the Escherichia coli ribosomal termination complex with release factor 2. Klaholz, Bruno P.; Pape, Tillmann; Zavialov, Andrey V.; Myasnikov, Alexander G.; Orlova, Elena V.; Vestergaard, Bente; Ehrenberg, Måns; van Heel, Marin // Nature;1/2/2003, Vol. 421 Issue 6918, p90 

    Termination of protein synthesis[SUP1] occurs when the messenger RNA presents a stop codon in the ribosomal aminoacyl (A) site. Class I release factor proteins (RF1 or RF2) are believed to recognize stop codons via tripeptide motifs[SUP2], leading to release of the completed polypeptide chain...


Read the Article


Sorry, but this item is not currently available from your library.

Try another library?
Sign out of this library

Other Topics