Cold Adaptation of the Antarctic Archaeon,Methanococcoides burtoniiAssessed by Proteomics Using ICAT

2005 ◽  
Vol 4 (2) ◽  
pp. 473-480 ◽  
Author(s):  
Amber Goodchild ◽  
Mark Raftery ◽  
Neil F. W. Saunders ◽  
Michael Guilhaus ◽  
Ricardo Cavicchioli
Keyword(s):  
Cold Adaptation ◽  
The Antarctic

Ribosomal cold-adaptation: Characterization of the genes encoding the acidic ribosomal P0 and P2 proteins from the Antarctic ciliate Euplotes focardii

Gene ◽  
2005 ◽  
Vol 360 (2) ◽  
pp. 103-110 ◽  
Author(s):  
Sandra Pucciarelli ◽  
Francesca Marziale ◽  
Graziano Di Giuseppe ◽  
Sabrina Barchetta ◽  
Cristina Miceli
Keyword(s):  
Cold Adaptation ◽  
Genes Encoding ◽  
The Antarctic

Physiological reactions to cold of men in the Antarctic

1964 ◽  
Vol 19 (4) ◽  
pp. 593-597 ◽  
Author(s):  
C. H. Wyndham ◽  
R. Plotkin ◽  
A. Munro
Keyword(s):  
South African ◽  
Cold Adaptation ◽  
Physiological Responses ◽  
Control Group ◽  
Climatic Chamber ◽  
Thermoneutral Zone ◽  
The Antarctic ◽  
Physiological Reactions ◽  
Average Skin ◽  
Skin Temperatures

The physiological reactions to cold of five members of the 1961–1962 South African expedition to the Antarctic were studied in a climatic chamber in Johannesburg, and again after 6 months and after 12 months in the Antarctic. Their results were compared with the results of a control group in Johannesburg. The predeparture results were within the 95% significance intervals of the control group. After 12 months in the Antarctic their results fell outside the 95% significance intervals of the control group when at 5 C air temperature, metabolism, average skin temperatures, rectal temperatures, and finger temperatures were all significantly lower. Toe temperatures, however, were higher. There appeared to be a gradual “adaptation” and general “toughening” to the cold, because the subjects shed their clothing progressively until they could run about naked in the snow. The values at the thermoneutral zone of 27 C did not change over the 12 months, however. It is therefore concluded that it is unlikely that the changes in physiological responses were of endocrine origin. cold adaptation in Antarctic; metabolic and body temperature reactions to cold Submitted on August 16, 1963

A proteomic determination of cold adaptation in the Antarctic archaeon, Methanococcoides burtonii

2004 ◽  
Vol 53 (1) ◽  
pp. 309-321 ◽  
Author(s):  
Amber Goodchild ◽  
Neil F. W. Saunders ◽  
Haluk Ertan ◽  
Mark Raftery ◽  
Michael Guilhaus ◽  
...  
Keyword(s):  
Cold Adaptation ◽  
The Antarctic

Review: the Antarctic Chlamydomonas raudensis: an emerging model for cold adaptation of photosynthesis

Extremophiles ◽  
2013 ◽  
Vol 17 (5) ◽  
pp. 711-722 ◽  
Author(s):  
Jenna M. Dolhi ◽  
Denis P. Maxwell ◽  
Rachael M. Morgan-Kiss
Keyword(s):  
Cold Adaptation ◽  
Chlamydomonas Raudensis ◽  
The Antarctic

Is Gene Duplication Driving Cold Adaptation in the Antarctic Green Alga Chlamydomonas Sp. UWO241?

2020 ◽  
Author(s):  
Xi Zhang ◽  
Marina Cvetkovska ◽  
Rachael Morgan-Kiss ◽  
Norman P. A. Hüner ◽  
David Roy Smith
Keyword(s):  
Gene Duplication ◽  
Green Alga ◽  
Cold Adaptation ◽  
The Antarctic

The heart of the Antarctic icefish as paradigm of cold adaptation

1997 ◽  
Vol 22 (6) ◽  
pp. 409-417 ◽  
Author(s):  
B. Tota ◽  
M.C. Cerra ◽  
R. Mazza ◽  
D. Pellegrino ◽  
J. Icardo
Keyword(s):  
Cold Adaptation ◽  
Antarctic Icefish ◽  
The Antarctic

Cold adaptation of the antarctic fish Trematomus bernacchii

1968 ◽  
Vol 26 (1) ◽  
pp. 223-233 ◽  
Author(s):  
George N. Somero ◽  
Arthur C. Giese ◽  
Donald E. Wohlschlag
Keyword(s):  
Cold Adaptation ◽  
Antarctic Fish ◽  
Trematomus Bernacchii ◽  
The Antarctic

Absence of metabolic cold adaptation and compensatory acclimation in the Antarctic fly, Belgica antarctica

1982 ◽  
Vol 28 (9) ◽  
pp. 725-729 ◽  
Author(s):  
Richard E. Lee ◽  
John G. Baust
Keyword(s):  
Cold Adaptation ◽  
Belgica Antarctica ◽  
The Antarctic ◽  
Metabolic Cold Adaptation

scholarly journals Cold adaptation of proteins. Purification, characterization, and sequence of the heat-labile subtilisin from the antarctic psychrophile Bacillus TA41

1994 ◽  
Vol 269 (26) ◽  
pp. 17448-17453 ◽  
Author(s):  
S. Davail ◽  
G. Feller ◽  
E. Narinx ◽  
C. Gerday
Keyword(s):  
Cold Adaptation ◽  
Heat Labile ◽  
The Antarctic

scholarly journals An In-Silico Comparative Study of Lipases from the Antarctic Psychrophilic Ciliate Euplotes focardii and the Mesophilic Congeneric Species Euplotes crassus: Insight into Molecular Cold-Adaptation

Marine Drugs ◽  
2021 ◽  
Vol 19 (2) ◽  
pp. 67
Author(s):  
Guang Yang ◽  
Matteo Mozzicafreddo ◽  
Patrizia Ballarini ◽  
Sandra Pucciarelli ◽  
Cristina Miceli
Keyword(s):  
Amino Acid ◽  
Low Temperatures ◽  
In Silico ◽  
Cold Adaptation ◽  
Structural Changes ◽  
Hydrolytic Enzymes ◽  
Industrial Applications ◽  
Euplotes Crassus ◽  
Ciliate Species ◽  
The Antarctic

Cold-adapted enzymes produced by psychrophilic organisms have elevated catalytic activities at low temperatures compared to their mesophilic counterparts. This is largely due to amino acids changes in the protein sequence that often confer increased molecular flexibility in the cold. Comparison of structural changes between psychrophilic and mesophilic enzymes often reveal molecular cold adaptation. In the present study, we performed an in-silico comparative analysis of 104 hydrolytic enzymes belonging to the family of lipases from two evolutionary close marine ciliate species: The Antarctic psychrophilic Euplotes focardii and the mesophilic Euplotes crassus. By applying bioinformatics approaches, we compared amino acid composition and predicted secondary and tertiary structures of these lipases to extract relevant information relative to cold adaptation. Our results not only confirm the importance of several previous recognized amino acid substitutions for cold adaptation, as the preference for small amino acid, but also identify some new factors correlated with the secondary structure possibly responsible for enhanced enzyme activity at low temperatures. This study emphasizes the subtle sequence and structural modifications that may help to transform mesophilic into psychrophilic enzymes for industrial applications by protein engineering.

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