Agl22 and Agl23 are involved in the synthesis and utilization of the lipid‐linked intermediates in the glycosylation pathways of the halophilic archaeaon Haloarcula hispanica

2020 ◽  
Vol 114 (5) ◽  
pp. 762-774 ◽  
Author(s):  
Hua Lu ◽  
Caixia Pei ◽  
Hui Zhou ◽  
Yang Lü ◽  
Yun He ◽  
...  
Keyword(s):  
Haloarcula Hispanica

scholarly journals Multiple replication origins with diverse control mechanisms in Haloarcula hispanica

2013 ◽  
Vol 42 (4) ◽  
pp. 2282-2294 ◽  
Author(s):  
Zhenfang Wu ◽  
Jingfang Liu ◽  
Haibo Yang ◽  
Hailong Liu ◽  
Hua Xiang
Keyword(s):  
Replication Initiation ◽  
Control Mechanisms ◽  
Replication Origins ◽  
Dna Mutation ◽  
Genome Wide ◽  
Marker Frequency ◽  
Haloarcula Hispanica ◽  
Specific Control ◽  
Main Chromosome ◽  
Multiple Replication

Abstract The use of multiple replication origins in archaea is not well understood. In particular, little is known about their specific control mechanisms. Here, we investigated the active replication origins in the three replicons of a halophilic archaeon, Haloarcula hispanica, by extensive gene deletion, DNA mutation and genome-wide marker frequency analyses. We revealed that individual origins are specifically dependent on their co-located cdc6 genes, and a single active origin/cdc6 pairing is essential and sufficient for each replicon. Notably, we demonstrated that the activities of oriC1 and oriC2, the two origins on the main chromosome, are differently controlled. A G-rich inverted repeat located in the internal region between the two inverted origin recognition boxes (ORBs) plays as an enhancer for oriC1, whereas the replication initiation at oriC2 is negatively regulated by an ORB-rich region located downstream of oriC2-cdc6E, likely via Cdc6E-titrating. The oriC2 placed on a plasmid is incompatible with the wild-type (but not the ΔoriC2) host strain, further indicating that strict control of the oriC2 activity is important for the cell. This is the first report revealing diverse control mechanisms of origins in haloarchaea, which has provided novel insights into the use and coordination of multiple replication origins in the domain of Archaea.

Production of α-Amylase from Haloarcula hispanica 2TK2 Strain: Optimization of the Parameters That Effecting Activity

2013 ◽  
Vol 19 (12) ◽  
pp. 3551-3555 ◽  
Author(s):  
Aytun Nilay Erdagi ◽  
Azade Attar ◽  
Yeliz Basaran-Elalmis ◽  
Sevil Yucel ◽  
Meral Birbir
Keyword(s):  
Strain Optimization ◽  
Haloarcula Hispanica

scholarly journals An Acidic Exopolysaccharide fromHaloarcula hispanicaATCC33960 and Two Genes Responsible for Its Synthesis

Archaea ◽  
2017 ◽  
Vol 2017 ◽  
pp. 1-12 ◽  
Author(s):  
Yang Lü ◽  
Hua Lu ◽  
Shiwei Wang ◽  
Jing Han ◽  
Hua Xiang ◽  
...  
Keyword(s):  
Cell Surface ◽  
Surface Morphology ◽  
Harsh Environments ◽  
Molar Ratio ◽  
Swimming Ability ◽  
Halophilic Archaeon ◽  
Retarded Growth ◽  
Extremely Halophilic Archaeon ◽  
Haloarcula Hispanica ◽  
Cell Surface Morphology

A 1.1 × 106 Da acidic exopolysaccharide (EPS) was purified from an extremely halophilic archaeonHaloarcula hispanicaATCC33960 with a production of 30 mg L−1when grown in AS-168 medium, which mainly composed of mannose and galactose with a small amount of glucose in a molar ratio of 55.9 : 43.2 : 0.9. Two glycosyltransferase genes (HAH_1662andHAH_1667) were identified to be responsible for synthesis of the acidic EPS. Deletion of eitherHAH_1662orHAH_1667led to loss of the acidic EPS. The mutants displayed a different cell surface morphology, retarded growth in low salty environment, an increased adhesion, and swimming ability. Our results suggest that biosynthesis of the acidic EPS might act as an adaptable mechanism to protect the cells against harsh environments.

scholarly journals Haloarcula mannanilytica sp. nov., a galactomannan-degrading haloarchaeon isolated from commercial salt

2020 ◽  
Vol 70 (12) ◽  
pp. 6331-6337 ◽  
Author(s):  
Shigeaki Enomoto ◽  
Yasuhiro Shimane ◽  
Kunio Ihara ◽  
Masahiro Kamekura ◽  
Takashi Itoh ◽  
...  
Keyword(s):  
Type Species ◽  
Phylogenetic Analyses ◽  
Rrna Gene ◽  
Content Type ◽  
Haloarcula Japonica ◽  
Link Type ◽  
Ishikawa Prefecture ◽  
Haloarcula Hispanica ◽  
A New Species ◽  
Made In

A mannan-degrading halophilic archaeal strain, MD130-1T, was isolated from a commercial salt sample. Cells were motile, rod-shaped, and stained Gram-negative. Colonies were pink pigmented. Strain MD130-1T was able to grow at 1.5–4.6 M NaCl (optimum, 3.6 M) at pH 6.0–8.0 (optimum, pH 7.0) and at 25–50 °C (optimum, 40 °C). The DNA G+C content was 62.1 mol% (genome). The orthologous 16S rRNA gene sequence showed the highest similarity (99.4 %) to those of Haloarcula japonica JCM 7785T and Haloarcula hispanica JCM 8911T. The values of genome relatedness between strain MD130-1T and Haloarcula species were 84.33–85.96 % in ANIb and 30.4–32.9 % using GGDC formula 2. The polar lipids of strain MD130-1T were phosphatidylglycerol, phosphatidylglycerol phosphate methyl ester and triglycosyl diether-2. Based on the results of phenotypic and phylogenetic analyses, the strain represents a new species of the genus Haloarcula , for which the name Haloarcula mannanilytica sp. nov. is proposed. The type strain is MD130-1T (=JCM 33835T=KCTC 4287T) isolated from commercial salt made in Ishikawa prefecture, Japan.

scholarly journals An Improved Transposon for the Halophilic ArchaeonHaloarcula hispanica

1999 ◽  
Vol 181 (22) ◽  
pp. 7140-7142 ◽  
Author(s):  
Wayne G. Woods ◽  
Katrina Ngui ◽  
Michael L. Dyall-Smith
Keyword(s):  
Insertion Sequence ◽  
Target Sequence ◽  
Sequence Specificity ◽  
Haloarcula Hispanica

ABSTRACT An improved transposon (ThD73) for Haloarcula hispanica is described. Based on the halobacterial insertion sequence ISH28, it showed little target sequence specificity but was biased toward a lower G+C content. Twenty randomly selected ThD73 mutants were analyzed, and the DNA flanking their insertions revealed several recognizable sequences, including two (unrelated) ISH elements.

scholarly journals Halobacterium salinarum virus ChaoS9, a Novel Halovirus Related to PhiH1 and PhiCh1

Genes ◽  
2019 ◽  
Vol 10 (3) ◽  
pp. 194 ◽  
Author(s):  
Mike Dyall-Smith ◽  
Peter Palm ◽  
Gerhard Wanner ◽  
Angela Witte ◽  
Dieter Oesterhelt ◽  
...  
Keyword(s):  
Unit Length ◽  
Halobacterium Salinarum ◽  
Tail Fiber ◽  
Homogeneous Population ◽  
Head Assembly ◽  
Linear Dsdna ◽  
Natrialba Magadii ◽  
The Right ◽  
Haloarcula Hispanica ◽  
Assembly Proteins

The unexpected lysis of a large culture of Halobacterium salinarum strain S9 was found to be caused by a novel myovirus, designated ChaoS9. Virus purification from the culture lysate revealed a homogeneous population of caudovirus-like particles. The viral genome is linear, dsDNA that is partially redundant and circularly permuted, has a unit length of 55,145 nt, a G + C% of 65.3, and has 85 predicted coding sequences (CDS) and one tRNA (Arg) gene. The left arm of the genome (0–28 kbp) encodes proteins similar in sequence to those from known caudoviruses and was most similar to myohaloviruses phiCh1 (host: Natrialba magadii) and phiH1 (host: Hbt. salinarum). It carries a tail-fiber gene module similar to the invertible modules present in phiH1 and phiCh1. However, while the tail genes of ChaoS9 were similar to those of phiCh1 and phiH1, the Mcp of ChaoS9 was most similar (36% aa identity) to that of Haloarcula hispanica tailed virus 1 (HHTV-1). Provirus elements related to ChaoS9 showed most similarity to tail/assembly proteins but varied in their similarity with head/assembly proteins. The right arm (29–55 kbp) of ChaoS9 encoded proteins involved in DNA replication (ParA, RepH, and Orc1) but the other proteins showed little similarity to those from phiH1, phiCh1, or provirus elements, and most of them could not be assigned a function. ChaoS9 is probably best classified within the genus Myohalovirus, as it shares many characteristics with phiH1 (and phiCh1), including many similar proteins. However, the head/assembly gene region appears to have undergone a recombination event, and the inferred proteins are different to those of phiH1 and phiCh1, including the major capsid protein. This makes the taxonomic classification of ChaoS9 more ambiguous. We also report a revised genome sequence and annotation of Natrialba virus phiCh1.

scholarly journals Constituents of SH1, a Novel Lipid-Containing Virus Infecting the Halophilic Euryarchaeon Haloarcula hispanica

2005 ◽  
Vol 79 (14) ◽  
pp. 9097-9107 ◽  
Author(s):  
Dennis H. Bamford ◽  
Janne J. Ravantti ◽  
Gunilla Rönnholm ◽  
Simonas Laurinavičius ◽  
Petra Kukkaro ◽  
...  
Keyword(s):  
Common Ancestor ◽  
Sequence Similarity ◽  
Open Reading Frames ◽  
Structural Components ◽  
Main Interest ◽  
Double Stranded Dna ◽  
Archaeal Viruses ◽  
Dsdna Viruses ◽  
Haloarcula Hispanica ◽  
Reading Frames

ABSTRACT Recent studies have indicated that a number of bacterial and eukaryotic viruses that share a common architectural principle are related, leading to the proposal of an early common ancestor. A prediction of this model would be the discovery of similar viruses that infect archaeal hosts. Our main interest lies in icosahedral double-stranded DNA (dsDNA) viruses with an internal membrane, and we now extend our studies to include viruses infecting archaeal hosts. While the number of sequenced archaeal viruses is increasing, very little sequence similarity has been detected between bacterial and eukaryotic viruses. In this investigation we rigorously show that SH1, an icosahedral dsDNA virus infecting Haloarcula hispanica, possesses lipid structural components that are selectively acquired from the host pool. We also determined the sequence of the 31-kb SH1 genome and positively identified genes for 11 structural proteins, with putative identification of three additional proteins. The SH1 genome is unique and, except for a few open reading frames, shows no detectable similarity to other published sequences, but the overall structure of the SH1 virion and its linear genome with inverted terminal repeats is reminiscent of lipid-containing dsDNA bacteriophages like PRD1.

scholarly journals Enzymatic activity of a novel halotolerant lipase from Haloarcula hispanica 2TK2

2016 ◽  
Vol 18 (2) ◽  
pp. 20-25 ◽  
Author(s):  
Melis Ozgen ◽  
Azade Attar ◽  
Yeliz Elalmis ◽  
Meral Birbir ◽  
Sevil Yucel
Keyword(s):  
Salt Concentration ◽  
Lipolytic Activity ◽  
Carbon Sources ◽  
Lipase Production ◽  
Relative Activity ◽  
Walnut Oil ◽  
Nacl Concentration ◽  
Potential Applications ◽  
Triton X ◽  
Haloarcula Hispanica

Abstract A strain of Haloarcula hispanica isolated from Tuzkoy salt mine, Turkey exhibited extracellular lipolytic activity. Important parameters such as carbon sources and salt concentration for lipase production were investigated. Optimal conditions for the enzyme production from Haloarcula hispanica 2TK2 were determined. It was observed that the lipolytic activity of Haloarcula hispanica was stimulated by some of the carbon sources. The high lipase acitivity values were obtained in the presence of 2% (v/v) walnut oil (6.16 U/ml), 1% (v/v) fish oil (5.07 U/ml), 1% (v/v) olive oil (4.52 U/ml) and 1% (w/v) stearic acid (4.88 U/ml) at 4M NaCl concentration. Lipase was partially purified by ammonium sulfate precipitation and ultrafiltration. Optimal temperature and pH values were determined as 45°C and 8.0, respectively. Lipase activity decreased with the increasing salt concentration, but 85% activity of the enzyme was maintained at 5M NaCl concentration. The enzyme preserved 41% of its relative activity at 90°C. The partially purified lipase maintained its activity in the presence of surfactants such as Triton X-100 and SDS. Therefore, the lipase which is an extremozyme may have potential applications especially in detergent industry.

scholarly journals Vesicle-like virion of Haloarcula hispanica pleomorphic virus 3 preserves high infectivity in saturated salt

Virology ◽  
2016 ◽  
Vol 499 ◽  
pp. 40-51 ◽  
Author(s):  
Tatiana A. Demina ◽  
Nina S. Atanasova ◽  
Maija K. Pietilä ◽  
Hanna M. Oksanen ◽  
Dennis H. Bamford
Keyword(s):  
Haloarcula Hispanica ◽  
High Infectivity
Sign in / Sign up

Export Citation Format

Share Document