Understanding Life at High Temperatures: Relationships of Molecular Channels in Enzymes of Methanogenic Archaea and Their Growth Temperatures

被引:0
|
作者
Ginsbach, Laura F. [1 ]
Gonzalez, Juan M. [2 ]
机构
[1] Tech Univ Berlin, Inst Biotechnol, Dept Appl Biochem, D-10623 Berlin, Germany
[2] CSIC, Inst Recursos Nat & Agrobiol Sevilla, IRNAS CSIC, Seville 41012, Spain
关键词
molecular channels; molecular tunnels; hyperthermophiles; thermal stability; methanogen; Archaea; GLUTAMATE-DEHYDROGENASE; STABILITY; TUNNELS;
D O I
10.3390/ijms232315149
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Analyses of protein structures have shown the existence of molecular channels in enzymes from Prokaryotes. Those molecular channels suggest a critical role of spatial voids in proteins, above all, in those enzymes functioning under high temperature. It is expected that these spaces within the protein structure are required to access the active site and to maximize availability and thermal stability of their substrates and cofactors. Interestingly, numerous substrates and cofactors have been reported to be highly temperature-sensitive biomolecules. Methanogens represent a singular phylogenetic group of Archaea that performs anaerobic respiration producing methane during growth. Methanogens inhabit a variety of environments including the full range of temperatures for the known living forms. Herein, we carry out a dimensional analysis of molecular tunnels in key enzymes of the methanogenic pathway from methanogenic Archaea growing optimally over a broad temperature range. We aim to determine whether the dimensions of the molecular tunnels are critical for those enzymes from thermophiles. Results showed that at increasing growth temperature the dimensions of molecular tunnels in the enzymes methyl-coenzyme M reductase and heterodisulfide reductase become increasingly restrictive and present strict limits at the highest growth temperatures, i.e., for hyperthermophilic methanogens. However, growth at lower temperature allows a wide dimensional range for the molecular spaces in these enzymes. This is in agreement with previous suggestions on a potential major role of molecular tunnels to maintain biomolecule stability and activity of some enzymes in microorganisms growing at high temperatures. These results contribute to better understand archaeal growth at high temperatures. Furthermore, an optimization of the dimensions of molecular tunnels would represent an important adaptation required to maintain the activity of key enzymes of the methanogenic pathway for those methanogens growing optimally at high temperatures.
引用
收藏
页数:9
相关论文
共 50 条
  • [1] Life at High Temperatures
    Maheshwari, Ramesh
    RESONANCE-JOURNAL OF SCIENCE EDUCATION, 2005, 10 (09): : 23 - 36
  • [2] Life at high temperatures
    Ramesh Maheshwari
    Resonance, 2005, 10 (9) : 23 - 36
  • [3] LIFE AT HIGH-TEMPERATURES
    BROCK, TD
    SCIENCE, 1985, 230 (4722) : 132 - 138
  • [4] Molecular beam epitaxy and doping of AlN at high growth temperatures
    Boger, R.
    Fiederle, M.
    Kirste, L.
    Maier, M.
    Wagner, J.
    JOURNAL OF PHYSICS D-APPLIED PHYSICS, 2006, 39 (21) : 4616 - 4620
  • [5] Relationships of critical temperatures to calculated molecular properties
    Katritzky, AR
    Mu, L
    Karelson, M
    JOURNAL OF CHEMICAL INFORMATION AND COMPUTER SCIENCES, 1998, 38 (02): : 293 - 299
  • [6] MOLECULAR INTERACTIONS AT HIGH TEMPERATURES
    TREANOR, CE
    SKINNER, GT
    PLANETARY AND SPACE SCIENCE, 1961, 3 : 253 - 256
  • [7] CRYSTAL GROWTH AT HIGH TEMPERATURES
    ZERFOSS, S
    JOHNSON, LR
    EGLI, PH
    DISCUSSIONS OF THE FARADAY SOCIETY, 1949, (05): : 166 - 172
  • [8] PHYSIOLOGY OF GROWTH AT HIGH TEMPERATURES
    CAMPBELL, LL
    PACE, B
    JOURNAL OF APPLIED BACTERIOLOGY, 1968, 31 (01): : 24 - &
  • [9] The denaturation and degradation of stable enzymes at high temperatures
    Daniel, RM
    Dines, M
    Petach, HH
    BIOCHEMICAL JOURNAL, 1996, 317 : 1 - 11
  • [10] Biomolecular stability and life at high temperatures
    Daniel, RM
    Cowan, DA
    CELLULAR AND MOLECULAR LIFE SCIENCES, 2000, 57 (02) : 250 - 264