scholarly journals The cold adaption profiles of Pseudoalteromonas shioyasakiensis D1497 from Yap trench to cope with cold

2021 ◽  
pp. e00689
Author(s):  
Jingjing Duan ◽  
Wenbin Guo
Keyword(s):  
Cold Adaption

scholarly journals Cold-Active β-Galactosidases: Insight into Cold Adaption Mechanisms and Biotechnological Exploitation

Marine Drugs ◽  
2021 ◽  
Vol 19 (1) ◽  
pp. 43
Author(s):  
Marco Mangiagalli ◽  
Marina Lotti
Keyword(s):  
Low Temperature ◽  
Molecular Mechanisms ◽  
Building Blocks ◽  
Cold Active ◽  
Cold Adaption ◽  
Glycosyl Donor ◽  
Pharmaceutical Industries ◽  
Biotechnological Processes ◽  
Hydrolysis Of ◽  
Insight Into

β-galactosidases (EC 3.2.1.23) catalyze the hydrolysis of β-galactosidic bonds in oligosaccharides and, under certain conditions, transfer a sugar moiety from a glycosyl donor to an acceptor. Cold-active β-galactosidases are identified in microorganisms endemic to permanently low-temperature environments. While mesophilic β-galactosidases are broadly studied and employed for biotechnological purposes, the cold-active enzymes are still scarcely explored, although they may prove very useful in biotechnological processes at low temperature. This review covers several issues related to cold-active β-galactosidases, including their classification, structure and molecular mechanisms of cold adaptation. Moreover, their applications are discussed, focusing on the production of lactose-free dairy products as well as on the valorization of cheese whey and the synthesis of glycosyl building blocks for the food, cosmetic and pharmaceutical industries.

scholarly journals Structure and dynamics of a cold-active esterase reveals water entropy and active site accessibility as the likely drivers for cold-adaptation

2021 ◽  
Author(s):  
Nehad Noby ◽  
Husam Sabah Auhim ◽  
Rachel L. Johnson ◽  
Harley Worthy ◽  
Amira M. Embaby ◽  
...  
Keyword(s):  
Active Site ◽  
Cold Adaptation ◽  
Normal Mode Analysis ◽  
Hydrophobic Effect ◽  
Mode Analysis ◽  
Water Solvent ◽  
Rigidity Analysis ◽  
Helical Content ◽  
Cold Active ◽  
Cold Adaption

AbstractCold-active esterases hold great potential for undertaking useful biotransformations at low temperatures. Here, we determined the structure of a cold active family IV esterase (EstN7) cloned from Bacillus cohnii strain N1, which has an apparent melting temperature of 26°C. EstN7 is a dimer with a classical α/β hydrolase fold. It has an acidic surface that is thought to play a role in cold-adaption by retaining solvation under changed water solvent entropy at lower temperatures. However, dynamics do not appear to play a major role in cold adaption. Comparison of B-factors with the closest related mesophilic and thermophilic esterases suggests there is little difference in dynamics with the catalytically important N-terminal cap comprising the main dynamic element. Molecular dynamics, rigidity analysis, normal mode analysis and geometric simulations of motion confirm the flexibility of the cap region but suggest that the rest of the protein is largely rigid. Rigidity analysis indicates the distribution of hydrophobic tethers is appropriate to colder conditions, where the hydrophobic effect is weaker than in mesophilic conditions due to reduced water entropy. The conformation of the cap region is significantly different to EstN7’s closest relatives, forming a bridge-like structure with reduced helical content providing more than one access tunnel through to the active site. Thus, it is likely that increased substrate accessibility and tolerance to changes in water entropy are the main drivers of EstN7’s cold adaptation rather than changes in dynamics.

scholarly journals Data-Independent Acquisition-Based Proteome and Phosphoproteome Profiling Reveals Early Protein Phosphorylation and Dephosphorylation Events in Arabidopsis Seedlings upon Cold Exposure

2021 ◽  
Vol 22 (23) ◽  
pp. 12856
Author(s):  
Jinjuan Tan ◽  
Zhongjing Zhou ◽  
Hanqian Feng ◽  
Jiayun Xing ◽  
Yujie Niu ◽  
...  
Keyword(s):  
Protein Phosphorylation ◽  
Molecular Mechanisms ◽  
Cold Treatment ◽  
Temperature Drop ◽  
Mass Spectrometry Analysis ◽  
Cold Response ◽  
E3 Ligases ◽  
Data Independent Acquisition ◽  
Early Protein ◽  
Cold Adaption

Protein phosphorylation plays an important role in mediating signal transduction in cold response in plants. To better understand how plants sense and respond to the early temperature drop, we performed data-independent acquisition (DIA) method-based mass spectrometry analysis to profile the proteome and phosphoproteome of Arabidopsis seedlings upon cold stress in a time-course manner (10, 30 and 120 min of cold treatments). Our results showed the rapid and extensive changes at the phosphopeptide levels, but not at the protein abundance levels, indicating cold-mediated protein phosphorylation and dephosphorylation events. Alteration of over 1200 proteins at phosphopeptide levels were observed within 2 h of cold treatment, including over 140 kinases, over 40 transcriptional factors and over 40 E3 ligases, revealing the complexity of regulation of cold adaption. We summarized cold responsive phosphoproteins involved in phospholipid signaling, cytoskeleton reorganization, calcium signaling, and MAPK cascades. Cold-altered levels of 73 phosphopeptides (mostly novel cold-responsive) representing 62 proteins were validated by parallel reaction monitoring (PRM). In summary, this study furthers our understanding of the molecular mechanisms of cold adaption in plants and strongly supports that DIA coupled with PRM are valuable tools in uncovering early signaling events in plants.

scholarly journals Microarray transcriptional profiling of Arctic Mesorhizobium strain N33 at low temperature provides insights into cold adaption strategies

BMC Genomics ◽  
2015 ◽  
Vol 16 (1) ◽  
Author(s):  
Abdollah-Fardin Ghobakhlou ◽  
Anne Johnston ◽  
Linda Harris ◽  
Hani Antoun ◽  
Serge Laberge
Keyword(s):  
Low Temperature ◽  
Transcriptional Profiling ◽  
Cold Adaption
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