Abstract
We found that non-bleached and cyclically bleached tissues of X. muta harbored a unique Crenarchaeota community closely related to those reported for other sponges. In contrast, bleached tissue from the most degraded sponge contained a Crenarchaeota community that was more similar to those found in...
|
PMID: 20390264
PDF is available here.
Abstract
A haloalkaliphilic archaeon, strain JX313(T), was isolated from a saline-alkaline soil from Daqing, Heilongjiang Province, China. Its morphological, physiological and biochemical features and 16S rRNA gene sequence were determined. Colonies of the strain were orange-red and cells were non-motile coc...
|
PMID: 19915113
PDF is available here.
Abstract
A halophilic archaeon, strain RO1-6(T), was isolated from a marine solar saltern in eastern China. Cells of strain RO1-6(T) were pleomorphic and motile and stained Gram-negative. Strain RO1-6(T) grew well on complex medium and colonies were red-pigmented. It was able to grow at 20-50°C (optimum 37...
|
PMID: 19946053
PDF is available here.
Abstract
We determined the crystal structures of the archaeal tRNA(Sec).PSTK complex. PSTK consists of two independent linker-connected domains, the N-terminal catalytic domain (NTD) and the C-terminal domain (CTD). The D-arm.CTD binding occurs independently of and much more strongly than the acceptor-arm.NT...
|
PMID: 20705242
PDF is available here.
Abstract
We studied the substrate specificity of the exosome of Sulfolobus solfataricus using the catalytically active Rrp41-Rrp42-hexamer and complexes containing the RNA-binding subunits Rrp4 or Csl4. The conservation of both Rrp4 and Csl4 in archaeal and eukaryotic exosomes suggests specific functions for...
|
PMID: 20488184
PDF is available here.
Abstract
We present a novel strategy for evaluating the distribution of 3D motifs along the RNA chain and those motifs whose distributions are significantly non-random are identified. By applying it to the X-ray structure of the large ribosomal subunit from Haloarcula marismortui, helical motifs were found t...
|
PMID: 20159997
PDF is available here.
Abstract
We examined the functional equivalency between Escherichia coli RNase P protein (C5) and Pyrococcus horikoshii RNase P proteins (PhoPop5, PhoRpp21, PhoRpp29, PhoRpp30, and PhoRpp38) for RNase P activity. The C5 protein and P. horikoshii RNase P proteins were unable to activate non-congnate RNase P R...
|
PMID: 20139629
PDF is available here.
Abstract
The microbial community composition of colonized cotton and leachate samples from a landfill was quantified using small subunit (SSU) rRNA probes (quantitative rRNA hybridization). Relative quantification of bacteria, eukaryotes, and archaea revealed variations in the landfill microbial community be...
|
PMID: 20023104
PDF is available here.
Takuro Nunoura,
Hanako Oida,
Miwako Nakaseama,
Ayako Kosaka,
Satoru B Ohkubo,
Toru Kikuchi,
Hiromi Kazama,
Shoko Hosoi-Tanabe,
Ko-Ichi Nakamura,
Masataka Kinoshita,
Hisako Hirayama,
Fumio Inagaki,
Urumu Tsunogai,
Jun-Ichiro Ishibashi and
Ken Takai
Abstract
A variety of archaeal lineages have been identified using culture-independent molecular phylogenetic surveys of microbial habitats occurring in deep-sea hydrothermal environments such as chimney structures, sediments, vent emissions, and chemosynthetic macrofauna. With the exception of a few taxa, m...
|
PMID: 20023079
PDF is available here.
Abstract
We review the inner workings of this adaptable and heritable immune system and draw comparisons to small RNA-guided defense mechanisms in eukaryotic cells.
Copyright 2010 Elsevier Inc. All rights reserved....
|
PMID: 20129051
PDF is available here.
Abstract
A key element during the flow of genetic information in living systems is fidelity. The accuracy of DNA replication influences the genome size as well as the rate of genome evolution. The large amount of energy invested in gene expression implies that fidelity plays a major role in fitness. On the o...
|
PMID: 20871851
PDF is available here.
Abstract
The archaeal L7Ae and eukaryotic 15.5kD protein homologs are members of the L7Ae/15.5kD protein family that characteristically recognize K-turn motifs found in both archaeal and eukaryotic RNAs. In Archaea, the L7Ae protein uniquely binds the K-loop motif found in box C/D and H/ACA sRNAs, whereas th...
|
PMID: 19926724
PDF is available here.
Abstract
The recent discovery of protein modification by SAMPs, ubiquitin-like (Ubl) proteins from the archaeon Haloferax volcanii, prompted a comprehensive comparative-genomic analysis of archaeal Ubl protein genes and the genes for enzymes thought to be functionally associated with Ubl proteins. This analy...
|
PMID: 20936112
PDF is available here.
Abstract
We present a systematic study in which single C-terminal amino acid residues were added to a reporter protein and shown to influence its levels in an archaeal cell. All 20 amino acid residues were examined for their impact on protein levels, using the reporter protein soluble modified red-shifted GF...
|
PMID: 19850616
PDF is available here.
Abstract
Here we introduce an all-against-all sequence- and three-dimensional (3D) structure-based comparison of a representative set of RNA structures, which have allowed us to quantitatively confirm that: (i) there is a measurable relationship between sequence and structure conservation that weakens for al...
|
PMID: 20550657
PDF is available here.
Abstract
Small nucleolar RNAs (snoRNAs) are among the most evolutionarily ancient classes of small RNA. Two experimental screens published in BMC Genomics expand the eukaryotic snoRNA catalog, but many more snoRNAs remain to be found.
|
PMID: 20122292
PDF is available here.
Abstract
Microbial diversity in Movile Cave (Romania) was studied using bacterial and archaeal 16S rRNA gene sequence and functional gene analyses, including ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO), soxB (sulfate thioesterase/thiohydrolase) and amoA (ammonia monooxygenase). Sulfur oxidizers...
|
PMID: 19474813
PDF is available here.
Abstract
The prokaryotic diversity associated with organic household waste (OHW), leachate (start-up inoculum), and mesophilic anaerobic digestion processes in the degradation of OHW for 44 and 90 days was investigated using a culture-independent approach. Bacterial and archaeal 16S rRNA and mcrA gene clone...
|
PMID: 19551378
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.
Abstract
We show that SSO1450 is a high-affinity nucleic acid binding protein. It binds DNA, RNA and DNA-RNA hybrid apparently sequence non-specific in a multi-site binding mode. Furthermore, SSO1450 promotes the hybridization of complementary nucleic acid strands....
|
PMID: 19427858
PDF is available here.