Affiliation:
1. Laboratory of Molecular Biology
2. Department of Genetics, University of Wisconsin, Madison, Wisconsin 53706
Abstract
ABSTRACT
K
+
-selective ion channels (K
+
channels) have been found in bacteria, archaea, eucarya, and viruses. In
Paramecium
and other ciliates, K
+
currents play an essential role in cilia-based motility. We have retrieved and sequenced seven closely related
Paramecium
K
+
-channel gene (
PAK
) sequences by using previously reported fragments. An additional eight unique K
+
-channel sequences were retrieved from an indexed library recently used in a pilot genome sequencing project. Alignments of these protein translations indicate that while these 15 genes have diverged at different times, they all maintain many characteristics associated with just one subclass of metazoan K
+
channels (CNG/ERG type). Our results indicate that most of the genes are expressed, because all predicted frameshifts and several gaps in the homolog alignments contain
Paramecium
intron sequences deleted from reverse transcription-PCR products. Some of the variations in the 15 genomic nucleotide sequences involve an absence of introns, even between very closely related sequences, suggesting a potential occurrence of reverse transcription in the past. Extrapolation from the available genome sequence indicates that
Paramecium
harbors as many as several hundred of this one type of K
+
-channel gene. This quantity is far more numerous than those of K
+
-channel genes of all types known in any metazoan (e.g., ∼80 in humans, ∼30 in flies, and ∼15 in
Arabidopsis
). In an effort to understand this plurality, we discuss several possible reasons for their maintenance, including variations in expression levels in response to changes in the freshwater environment, like that seen with other major plasma membrane proteins in
Paramecium
.
Publisher
American Society for Microbiology
Subject
Molecular Biology,General Medicine,Microbiology
Reference38 articles.
1. Adoutte, A., K. Y. Ling, S. Chang, F. Huang, and C. Kung. 1983. Physiological and mutational protein variations in the ciliary membrane of Paramecium. Exp. Cell Res.148:387-404.
2. Ausubel F. M. R. Brent R. E. Kingston D. D. Moore J. G. Seidman J. A. Smith and K. Struhl (ed.). 2003. Current protocols in molecular biology. Greene Publishing Associates & Wiley Interscience New York N.Y.
3. Choe, S. 2002. Potassium channel structures. Nat. Rev. Neurosci.3:115-121.
4. Dessen, P., M. Zagulski, R. Gromadka, H. Plattner, R. Kissmehl, E. Meyer, M. Betermier, J. E. Schultz, J. U. Linder, R. E. Pearlman, C. Kung, J. Forney, B. H. Satir, J. L. Van Houten, A. M. Keller, M. Froissard, L. Sperling, and J. Cohen. 2001. Paramecium genome survey: a pilot project. Trends Genet.17:306-308.
5. Doyle, D. A., J. Morais Cabral, R. A. Pfuetzner, A. Kuo, J. M. Gulbis, S. L. Cohen, B. T. Chait, and R. MacKinnon. 1998. The structure of the potassium channel: molecular basis of K+ conduction and selectivity. Science280:69-77.
Cited by
24 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献