|
|
|
||||
| Home Help Feedback Subscriptions Archive Search | |||||
The fully linked HTML version of this article has now been published.
We screened the genomic sequences of the teleost fish Fugu rubripes for genes that encode cytoplasmic intermediate filament (IF) proteins. Here, we compare the number of genes per subfamily (I to IV) as well as the gene mapping in the human and fish genomes. There are several unexpected differences. F. rubripes has a sizeable excess of keratin type I genes over keratin type II genes. Four of the six keratin type II genes map close to four keratin type I genes. Thus, a single keratin II gene cluster (as in mammals) seems excluded. Although a continuous genome sequence is not yet available for F. rubripes, it is difficult to see how all 19 keratin type I genes can be collected as in the human genome into a single cluster without the presence of type II genes and various unrelated genes. F. rubripes has more type III and type IV genes than humans. Some of the type IV genes acquired additional novel intron positions. One gene even harbors (in addition to the two type IV introns) three novel introns and three introns usually present only in mammalian and F. rubripes type I-III genes. This mixture of type IV and type I-III intron positions poses a problem for the traditional view that the first type IV gene arose in evolution by a mRNA-mediated translocation event. In the 42 F. rubripes genes analysed here, there are several differences in intron patterns compared with mammalian genes. Most correspond to additional introns in the fish genes. A search for genes encoding nuclear lamins reveals the four established fish lamins (A, B1, B2 and LIII) as well as an unexpected second lamin A.
This article has been cited by other articles:
JCS ePress
online publication date 15 Apr 2003
doi: 10.1242/jcs.00444
This Article ![]()
![]()
Full Text (PDF)
![]()
All Versions of this Article:
jcs.00444v1
116/11/2295
most recent![]()
Alert me when this article is cited
![]()
Alert me if a correction is posted
![]()
Services ![]()
![]()
Email this article to a friend
![]()
Similar articles in this journal
![]()
Similar articles in PubMed
![]()
Alert me to new issues of the journal
![]()
Download to citation manager
![]()
![]()
Citing Articles ![]()
![]()
Citing Articles via HighWire
![]()
Citing Articles via Google Scholar
![]()
Google Scholar ![]()
![]()
Articles by Zimek, A. ![]()
Articles by Weber, K. ![]()
Search for Related Content
![]()
PubMed ![]()
![]()
PubMed Citation
![]()
Articles by Zimek, A.
![]()
Articles by Weber, K.
![]()
Social Bookmarking ![]()
![]()
What's this?
Research Article
Genes coding for intermediate filament proteins: common features and unexpected differences in the genomes of humans and the teleost fish Fugu rubripes
* Author for correspondence (e-mail: office.weber{at}mpibpc.gwdg.de)
![]()
CiteULike
Complore
Connotea
Del.icio.us
Digg
Reddit
Technorati
Twitter What's this?
![]()
![]()

![]()
![]()
![]()
L. Chang, K. Barlan, Y.-H. Chou, B. Grin, M. Lakonishok, A. S. Serpinskaya, D. K. Shumaker, H. Herrmann, V. I. Gelfand, and R. D. Goldman
The dynamic properties of intermediate filaments during organelle transport
J. Cell Sci.,
August 15, 2009;
122(16):
2914 - 2923.
[Abstract]
[Full Text]
[PDF]
![]()
![]()
![]()

![]()
![]()
![]()
D. D. Tang
Intermediate filaments in smooth muscle
Am J Physiol Cell Physiol,
April 1, 2008;
294(4):
C869 - C878.
[Abstract]
[Full Text]
[PDF]
![]()
![]()
![]()

![]()
![]()
![]()
M. S. Zastrow, S. Vlcek, and K. L. Wilson
Proteins that bind A-type lamins: integrating isolated clues
J. Cell Sci.,
March 1, 2004;
117(7):
979 - 987.
[Abstract]
[Full Text]
[PDF]
![]()
© The Company of Biologists Ltd 2003