Details
| Original language | English |
|---|---|
| Pages (from-to) | 32-6 |
| Number of pages | 5 |
| Journal | FEBS letters |
| Volume | 542 |
| Issue number | 1-3 |
| Publication status | Published - 8 May 2003 |
Abstract
Recently MjNhaP1 was identified as a pH-regulated Na(+)/H(+) antiporter of Methanococcus jannaschii [Hellmer, J. et al. (2002) FEBS Lett. 527, 245-249]. The antiporter is active at pH 6.0 and displays continuously decreasing activity towards alkaline pH. We have performed a site-directed mutagenesis study on all histidines as well as on conserved Asp, Glu and Arg residues of MjNhaP1, and analyzed the mutated proteins for activity. The mutants fall into three classes, i.e. normally active mutants, mutants with intermediate activity and mutants which are completely inactive. None of the histidine residues appears to be essential unlike in the bacterial proteins. The results point at an important role of a number of aspartate and arginine residues.
Keywords
- Amino Acid Sequence, Arginine/genetics, Aspartic Acid/genetics, Bacterial Proteins/chemistry, Hydrogen-Ion Concentration, Methanococcus/metabolism, Molecular Sequence Data, Mutagenesis, Site-Directed, Phylogeny, Sequence Alignment, Sodium-Hydrogen Exchangers/chemistry
Cite this
- Standard
- Harvard
- Apa
- Vancouver
- BibTeX
- RIS
In: FEBS letters, Vol. 542, No. 1-3, 08.05.2003, p. 32-6.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Conserved arginine and aspartate residues are critical for function of MjNhaP1, a Na+/H+ antiporter of M. jannaschii
AU - Hellmer, Jens
AU - Teubner, Andreas
AU - Zeilinger, Carsten
PY - 2003/5/8
Y1 - 2003/5/8
N2 - Recently MjNhaP1 was identified as a pH-regulated Na(+)/H(+) antiporter of Methanococcus jannaschii [Hellmer, J. et al. (2002) FEBS Lett. 527, 245-249]. The antiporter is active at pH 6.0 and displays continuously decreasing activity towards alkaline pH. We have performed a site-directed mutagenesis study on all histidines as well as on conserved Asp, Glu and Arg residues of MjNhaP1, and analyzed the mutated proteins for activity. The mutants fall into three classes, i.e. normally active mutants, mutants with intermediate activity and mutants which are completely inactive. None of the histidine residues appears to be essential unlike in the bacterial proteins. The results point at an important role of a number of aspartate and arginine residues.
AB - Recently MjNhaP1 was identified as a pH-regulated Na(+)/H(+) antiporter of Methanococcus jannaschii [Hellmer, J. et al. (2002) FEBS Lett. 527, 245-249]. The antiporter is active at pH 6.0 and displays continuously decreasing activity towards alkaline pH. We have performed a site-directed mutagenesis study on all histidines as well as on conserved Asp, Glu and Arg residues of MjNhaP1, and analyzed the mutated proteins for activity. The mutants fall into three classes, i.e. normally active mutants, mutants with intermediate activity and mutants which are completely inactive. None of the histidine residues appears to be essential unlike in the bacterial proteins. The results point at an important role of a number of aspartate and arginine residues.
KW - Amino Acid Sequence
KW - Arginine/genetics
KW - Aspartic Acid/genetics
KW - Bacterial Proteins/chemistry
KW - Hydrogen-Ion Concentration
KW - Methanococcus/metabolism
KW - Molecular Sequence Data
KW - Mutagenesis, Site-Directed
KW - Phylogeny
KW - Sequence Alignment
KW - Sodium-Hydrogen Exchangers/chemistry
U2 - 10.1016/s0014-5793(03)00332-6
DO - 10.1016/s0014-5793(03)00332-6
M3 - Article
C2 - 12729893
VL - 542
SP - 32
EP - 36
JO - FEBS letters
JF - FEBS letters
SN - 0014-5793
IS - 1-3
ER -