Halophilic adaptation of enzymes

Extremophiles ◽  
2000 ◽  
Vol 4 (2) ◽  
pp. 91-98 ◽  
Author(s):  
D. Madern ◽  
C. Ebel ◽  
G. Zaccai
Keyword(s):  
Halophilic Adaptation

Insights into the sequence parameters for halophilic adaptation

Amino Acids ◽  
2015 ◽  
Vol 48 (3) ◽  
pp. 751-762 ◽  
Author(s):  
Abhigyan Nath
Keyword(s):  
Sequence Parameters ◽  
Halophilic Adaptation

scholarly journals Dynamic structure mediates halophilic adaptation of a DNA polymerase from the deep‐sea brines of the Red Sea

2018 ◽  
Vol 32 (6) ◽  
pp. 3346-3360 ◽  
Author(s):  
Masateru Takahashi ◽  
Etsuko Takahashi ◽  
Luay I. Joudeh ◽  
Monica Marini ◽  
Gobind Das ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Red Sea ◽  
Deep Sea ◽  
Dynamic Structure ◽  
Halophilic Adaptation

scholarly journals Understanding High-Salt and Cold Adaptation of a Polyextremophilic Enzyme

2020 ◽  
Vol 8 (10) ◽  
pp. 1594 ◽  
Author(s):  
Ram Karan ◽  
Sam Mathew ◽  
Reyhan Muhammad ◽  
Didier B. Bautista ◽  
Malvina Vogler ◽  
...  
Keyword(s):  
Low Temperatures ◽  
Surface Acidity ◽  
Salt Content ◽  
Large Temperature ◽  
Structural Flexibility ◽  
X Ray Crystallography ◽  
Limited Protein ◽  
Dynamics Simulations ◽  
Exceptional Stability ◽  
Halophilic Adaptation

The haloarchaeon Halorubrum lacusprofundi is among the few polyextremophilic organisms capable of surviving in one of the most extreme aquatic environments on Earth, the Deep Lake of Antarctica (−18 °C to +11.5 °C and 21–28%, w/v salt content). Hence, H. lacusprofundi has been proposed as a model for biotechnology and astrobiology to investigate potential life beyond Earth. To understand the mechanisms that allow proteins to adapt to both salinity and cold, we structurally (including X-ray crystallography and molecular dynamics simulations) and functionally characterized the β-galactosidase from H. lacusprofundi (hla_bga). Recombinant hla_bga (produced in Haloferax volcanii) revealed exceptional stability, tolerating up to 4 M NaCl and up to 20% (v/v) of organic solvents. Despite being cold-adapted, hla_bga was also stable up to 60 °C. Structural analysis showed that hla_bga combined increased surface acidity (associated with halophily) with increased structural flexibility, fine-tuned on a residue level, for sustaining activity at low temperatures. The resulting blend enhanced structural flexibility at low temperatures but also limited protein movements at higher temperatures relative to mesophilic homologs. Collectively, these observations help in understanding the molecular basis of a dual psychrophilic and halophilic adaptation and suggest that such enzymes may be intrinsically stable and functional over an exceptionally large temperature range.

Halophilic Adaptation:  Novel Solvent Protein Interactions Observed in the 2.9 and 2.6 Å Resolution Structures of the Wild Type and a Mutant of Malate Dehydrogenase fromHaloarcula marismortui‡

Biochemistry ◽  
2000 ◽  
Vol 39 (5) ◽  
pp. 992-1000 ◽  
Author(s):  
Stéphane B. Richard ◽  
Dominique Madern ◽  
Elsa Garcin ◽  
Giuseppe Zaccai
Keyword(s):  
Malate Dehydrogenase ◽  
Protein Interactions ◽  
Wild Type ◽  
Halophilic Adaptation

Link between Protein−Solvent and Weak Protein−Protein Interactions Gives Insight into Halophilic Adaptation†

Biochemistry ◽  
2002 ◽  
Vol 41 (44) ◽  
pp. 13245-13252 ◽  
Author(s):  
Lionel Costenaro ◽  
Giuseppe Zaccai ◽  
Christine Ebel
Keyword(s):  
Protein Interactions ◽  
Protein Protein Interactions ◽  
Halophilic Adaptation ◽  
Insight Into

Halophilic adaptation of protein–DNA interactions

2003 ◽  
Vol 31 (3) ◽  
pp. 677-680 ◽  
Author(s):  
S. Bergqvist ◽  
M.A. Williams ◽  
R. O'Brien ◽  
J.E. Ladbury
Keyword(s):  
Dna Interaction ◽  
Dna Interactions ◽  
Evolutionary Time ◽  
Homologous Proteins ◽  
Binding Characteristics ◽  
Dna Binding Site ◽  
Protein Dna Interactions ◽  
Tata Box Binding Protein ◽  
Dna Complex ◽  
Halophilic Adaptation

Pyrococcus woesei (Pw) is an archaeal organism adapted to living in conditions of elevated salt and temperature. Thermodynamic data reveal that the interaction between the TATA-box-binding protein (TBP) from this organism and DNA has an entirely different character to the same interaction in mesophilic counterparts. In the case of the PwTBP, the affinity of its interaction with DNA increases with increasing salt concentration. The opposite effect is observed in all known mesophilic protein–DNA interactions. The halophilic behaviour can be attributed to sequestration of cations into the protein–DNA complex. By mutating residues in the PwTBP DNA-binding site, potential sites of cation interaction can be removed. These mutations have a significant effect on the binding characteristics, and the halophilic nature of the PwTBP–DNA interaction can be reversed, and made to resemble that of a mesophile, in just three mutations. The genes of functionally homologous proteins in organisms existing in different environments show that adaptation is most often accompanied by mutation of an existing protein. However, the importance of any individual residue to a phenotypic characteristic is usually difficult to assess amongst the multitude of changes that occur over evolutionary time. Since the halophilic nature of this protein can be attributed to only three mutations, this reveals that the important phenotype of halophilicity could be rapidly acquired in evolutionary time.

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