Protein thermostability in extremophiles

Scandurra, Roberto; Consalvi, Valerio; Chiaraluce, Roberta; Politi, Laura; Engel, Paul C.

doi:10.1016/s0300-9084(00)88890-2

Cited by 131 publications

(102 citation statements)

References 60 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…4C, inset). This value is similar to that observed with other thermophilic enzymes (33,54) and much higher that the 20 -40 kJ/mol energy of activation determined for mesophilic enzymes (46). Previous studies have indicated the dependence of CPxATPase activity on the presence of thiolates (20,30) and/or reducing agents (55,56).…”

Section: Characterization Of a Thermophilic Agsupporting

confidence: 89%

“…Proteins from hyperthermophile organisms, archaea in particular, have received significant attention because of their extraordinary stability (32,33). The study of thermotolerant, soluble proteins suggests that the intrinsic structure determined by the amino acid sequence is the determinant of their stability.…”

Section: P-type Atpases Transport a Variety Of Ions (Hmentioning

confidence: 99%

“…Although no particular stabilizing mechanism is obvious in these proteins, a general increment of small strengthening forces is apparent (hydrogen bonds, ion pairs, etc.). This structural stability appears to have been achieved at the expense of flexibility, since most of these enzymes are inactive under 40°C and have high activation energies (32,33). On the other hand, thermophilic membrane proteins and solute transporters in particular have received little attention.…”

Section: P-type Atpases Transport a Variety Of Ions (Hmentioning

confidence: 99%

See 2 more Smart Citations

Characterization of a Thermophilic P-type Ag+/Cu+-ATPase from the ExtremophileArchaeoglobus fulgidus

Mandal

Cheung²,

Argüello

2002

Journal of Biological Chemistry

123

192

View full text Add to dashboard Cite

The thermophilic, sulfur metabolizing Archaeoglobus fulgidus contains two genes, AF0473 and AF0152, encoding for PIB-type heavy metal transport ATPases. In this study, we describe the cloning, heterologous expression, purification, and functional characterization of one of these ATPases, CopA (NCB accession number AAB90763), encoded by AF0473. 50 ‫؍‬ 24 M). This is the first Ag ؉ /Cu ؉ -ATPase expressed and purified in a functional form. Thus, it provides a model for structurefunctional studies of these transporters. Moreover, its characterization will also contribute to an understanding of thermophilic ion transporters.

show abstract

Section: Characterization Of a Thermophilic Agsupporting

confidence: 89%

Section: P-type Atpases Transport a Variety Of Ions (Hmentioning

confidence: 99%

Section: P-type Atpases Transport a Variety Of Ions (Hmentioning

confidence: 99%

See 1 more Smart Citation

Characterization of a Thermophilic P-type Ag+/Cu+-ATPase from the ExtremophileArchaeoglobus fulgidus

Mandal

Cheung²,

Argüello

2002

Journal of Biological Chemistry

123

192

View full text Add to dashboard Cite

show abstract

“…The recently determined sequences and threedimensional structures of numerous proteins from moderate and extreme thermophiles have shed light on several factors that are used in different combinations and to different degrees by various proteins to increase their thermal stability. Stability mechanisms that have been implicated most often are increased ion pairing, hydrogen bonding, and compactness (36)(37)(38). The present study argues strongly that disulfide bonds are another important mechanism for achieving thermostability.…”

Section: Discussion Which Organisms Have Abundant Intracellular Disulmentioning

confidence: 55%

Genomic evidence that the intracellular proteins of archaeal microbes contain disulfide bonds

Mallick

Boutz

Eisenberg

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

168

145

View full text Add to dashboard Cite

Disulfide bonds have only rarely been found in intracellular proteins. That pattern is consistent with the chemically reducing environment inside the cells of well-studied organisms. However, recent experiments and new calculations based on genomic data of archaea provide striking contradictions to this pattern. Our results indicate that the intracellular proteins of certain hyperthermophilic archaea, especially the crenarchaea Pyrobaculum aerophilum and Aeropyrum pernix, are rich in disulfide bonds. This finding implicates disulfide bonding in stabilizing many thermostable proteins and points to novel chemical environments inside these microbes. These unexpected results illustrate the wealth of biochemical insights available from the growing reservoir of genomic data.

show abstract

“…17 Generally it is believed that the electrostatic interaction (include ion pairs and hydrogen bonds) and the hydrophobic interaction (nonpolar residue packing) in the proteins are the most important factors to protein thermostability (as well reviewed in [18][19][20][21][22] ). For the electrostatic interaction, Kumar et al have compared 18 nonredundant protein families of mesophilic and thermophilic proteins.…”

Section: Introductionmentioning

confidence: 99%

All‐atom contact potential approach to protein thermostability analysis

Chen

Xiao

2006

Biopolymers

View full text Add to dashboard Cite

In this paper we use all‐atom potential energy to define and analyze the inter‐residue contacts in mesophilic and thermophilic proteins. Fifteen families of proteins are selected and each family has two representative proteins with greatly different preferred environmental temperatures. We find that both the number and energy of the contacts defined in this way show stronger correlations with the preferred temperatures of proteins than other factors used before. We also find that the charged‐polar and charged‐nonpolar residue contacts not only have larger contact numbers but also have lower single contact energies. Furthermore, the most important is that most of the thermophilic proteins have more charged‐polar and charged‐nonpolar residue contacts than their mesophilic counterparts. This suggests that they may play an important role in the thermostability of proteins, except usual charged–charged and nonpolar–nonpolar residue contacts. Charged residues may exert their profound influence by forming contacts not only with other charged residues but also with polar or nonpolar residues, thus further increasing the strength of contact network and then the thermostability of proteins. © 2006 Wiley Periodicals, Inc. Biopolymers 85: 28–37, 2007.This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

show abstract

Protein thermostability in extremophiles

Cited by 131 publications

References 60 publications

Characterization of a Thermophilic P-type Ag+/Cu+-ATPase from the ExtremophileArchaeoglobus fulgidus

Characterization of a Thermophilic P-type Ag+/Cu+-ATPase from the ExtremophileArchaeoglobus fulgidus

Genomic evidence that the intracellular proteins of archaeal microbes contain disulfide bonds

All‐atom contact potential approach to protein thermostability analysis

Contact Info

Product

Resources

About