Halorubrum lacusprofundi
{{Short description|Species of archaeon}}
{{Speciesbox
| image = Halorubrum lacusprofundi ACAM34 (Anderson).png
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| taxon = Halorubrum lacusprofundi
| authority = Franzmann et al. 1989Page Species: Halorubrum lacusprofundi on {{cite web | url=https://lpsn.dsmz.de/species/halorubrum-lacusprofundi | title=LPSN - List of Prokaryotic names with Standing in Nomenclature | publisher=Deutsche Sammlung von Mikroorganismen und Zellkulturen | access-date=10 September 2022}}
| synonyms = {{Species list
|Halobacterium lacusprofundi|Franzmann et al. 1989Page Taxonomy browser (Halorubrum lacusprofundi) on {{cite web | url=https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=2247 | title=NCBI | access-date=10 September 2022}}
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Halorubrum lacusprofundi is a rod-shaped, halophilic Archaeon in the family of Halorubraceae. It was first isolated from Deep Lake in Antarctica in the 1980s.{{cite journal |vauthors= Franzmann PD, Stacklebrandt E, Sanderson K, Volkman JK, Camberon DE, Stevenson PL, McMeekin TA, Burton HR |year= 1988 |title= Halobacterium lacusprofundii sp. nov., a halophilic bacterium isolated from Deep Lake, Antarctica |journal=Systematic and Applied Microbiology |volume= 11 |issue= 1 |pages=20–27 |doi= 10.1016/S0723-2020(88)80044-4}}
Genome
Several strains of H. lacusprofundi have been discovered. The genome sequencing of the strain ACAM 32 was completed in 2008. The organism's genome consists of two circular chromosomes and a single circular plasmid. Chromosome I contains 2,735,295 base pairs encoding 2,801 genes and chromosome II contains 525,943 base pairs encoding 522 genes. The single plasmid contains 431,338 base pairs encoding 402 genes.{{cite journal |vauthors= Anderson IJ, DasSarma P, Lucas S, Copeland A, Lapidus A, Del Rio T, Tice H, Dalin E, Bruce DC, Goodwin L, Pitluck S, Sims D, Brettin TS, Detter JC, Han CS, Larimer F, Hauser L, Land M, Ivanova N, Richardson P, Cavicchioli R, DasSarma S, Woese CR, Kyrpides |year= 2016 |title= Complete genome sequence of the Antarctic Halorubrum lacusprofundi type strain ACAM 34 |journal= Standards in Genomic Sciences |volume= 11 |issue= 1 |pages= 70 |doi= 10.1186/s40793-016-0194-2 |pmc= 5018182 |pmid= 27617060 |doi-access= free }} At least one strain of H. lacusprofundi (R1S1) contains a plasmid (pR1SE) that enables horizontal gene transfer, which takes place via a mechanism that uses vesicle-enclosed virus-like particles.{{cite journal |vauthors=Erdmann S, Tschitschko B, Zhong L, Raftery MJ, Cavicchioli R |title=A plasmid from an Antarctic haloarchaeon uses specialized membrane vesicles to disseminate and infect plasmid-free cells|journal=Nature Microbiology|date=9 September 2017|volume=2|issue=10|pages=1446–1455|doi=10.1038/s41564-017-0009-2|pmid=28827601|s2cid=38729395|hdl=1959.4/unsworks_49908|hdl-access=free}}{{cite journal |vauthors=Gophna U, Altman-Price N |title=Horizontal Gene Transfer in Archaea—From Mechanisms to Genome Evolution |journal=Annual Review of Microbiology |volume=76 |issue=1 |date=8 September 2022 |issn=0066-4227 |doi=10.1146/annurev-micro-040820-124627 |pages=481–502|doi-access=free }}{{cite journal |vauthors=Gebhard LJ, Vershinin Z, Alarcón-Schumacher T, Eichler J, Erdmann S |title=Influence of N-Glycosylation on Virus-Host Interactions in Halorubrum lacusprofundi |journal=Viruses |volume=15 |issue=7 |date=June 2023 |page=1469 |pmid=37515157 |pmc=10384203 |doi=10.3390/v15071469 |doi-access=free }}
Research
Its β-galactosidase enzyme has been extensively studied to understand how proteins function in low-temperature, high-saline environments.{{cite journal |vauthors= Karan R, Capes MD, DasSarma P, DasSarma S |year= 2013 |title= Cloning, Overexpression, Purification, and Characterization of a Polyextremophilic β-galactosidase From the Antarctic Haloarchaeon Halorubrum lacusprofundi |journal= BMC Biotechnol. |volume= 13 |pages=10.1186/1472-6750-13-3 |doi= 10.1186/1472-6750-13-3 |pmc= 3556326 |pmid= 23320757 |doi-access= free }}{{cite journal |vauthors= Laye VJ, Karan R, Kim JM, Pecher WT, DasSarma P, DasSarma S |year= 2017 |title= Key amino acid residues conferring enhanced enzyme activity at cold temperatures in an Antarctic polyextremophilic β-galactosidase |journal= PNAS |volume= 114 |issue= 47 |pages= 12530–35 |doi= 10.1073/pnas.1711542114 |pmc= 5703305 |pmid= 29109294 |bibcode= 2017PNAS..11412530L |doi-access= free }}