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Kinetic behaviour of WT 1's zinc finger domain in binding to the alpha-actinin-1 mRNA.

Nurmemmedov, Elmar LU ; Kimbung, Raymond Yengo LU ; Ladomery, Michael R and Thunnissen, Marjolein LU (2010) In Archives of Biochemistry and Biophysics 497. p.21-27
Abstract
The zinc finger transcription factor Wilms tumour protein (WT 1) is known for its essential involvement in the development of the genitourinary system as well as of other organs and tissues. WT 1 is capable of selectively binding either DNA or mRNA targets. A KTS insertion due to alternative splicing between the zinc fingers 3 and 4 and an unconventional zinc finger 1 are the unique features that distinguish WT 1 from classical DNA-binding C(2)H(2)-type zinc finger proteins. The DNA binding characteristics of WT 1 are well studied. Due to lack of information about its native RNA targets, no extensive research has been directed at how WT 1 binds RNA. Using surface plasmon resonance, this study attempts to understand the binding behaviour of... (More)
The zinc finger transcription factor Wilms tumour protein (WT 1) is known for its essential involvement in the development of the genitourinary system as well as of other organs and tissues. WT 1 is capable of selectively binding either DNA or mRNA targets. A KTS insertion due to alternative splicing between the zinc fingers 3 and 4 and an unconventional zinc finger 1 are the unique features that distinguish WT 1 from classical DNA-binding C(2)H(2)-type zinc finger proteins. The DNA binding characteristics of WT 1 are well studied. Due to lack of information about its native RNA targets, no extensive research has been directed at how WT 1 binds RNA. Using surface plasmon resonance, this study attempts to understand the binding behaviour of WT 1 zinc fingers with its recently reported and first putative mRNA target, ACT 34, whose stem-loop structure is believed to be critical for the interactions with WT 1. We have analysed the interactions of five WT 1 zinc finger truncations with wild-type ACT 34 and four variants. Our results indicate that WT 1 zinc fingers bind ACT 34 in a specific manner, and that this occurs as interplay of all four zinc fingers. We also report that a sensitive kinetic balance, which is equilibrated by both zinc finger 1 and KTS, regulates the interaction with ACT 34. The stem-loop and the flanking nucleotides are important elements for specific recognition by WT 1 zinc fingers. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Archives of Biochemistry and Biophysics
volume
497
pages
21 - 27
publisher
Academic Press
external identifiers
  • wos:000277537800003
  • pmid:20193655
  • scopus:77952525574
ISSN
0003-9861
DOI
10.1016/j.abb.2010.02.013
language
English
LU publication?
yes
id
22cbbeac-1877-4935-af30-f93527136b9a (old id 1582704)
date added to LUP
2010-04-21 12:07:06
date last changed
2018-05-29 10:34:40
@article{22cbbeac-1877-4935-af30-f93527136b9a,
  abstract     = {The zinc finger transcription factor Wilms tumour protein (WT 1) is known for its essential involvement in the development of the genitourinary system as well as of other organs and tissues. WT 1 is capable of selectively binding either DNA or mRNA targets. A KTS insertion due to alternative splicing between the zinc fingers 3 and 4 and an unconventional zinc finger 1 are the unique features that distinguish WT 1 from classical DNA-binding C(2)H(2)-type zinc finger proteins. The DNA binding characteristics of WT 1 are well studied. Due to lack of information about its native RNA targets, no extensive research has been directed at how WT 1 binds RNA. Using surface plasmon resonance, this study attempts to understand the binding behaviour of WT 1 zinc fingers with its recently reported and first putative mRNA target, ACT 34, whose stem-loop structure is believed to be critical for the interactions with WT 1. We have analysed the interactions of five WT 1 zinc finger truncations with wild-type ACT 34 and four variants. Our results indicate that WT 1 zinc fingers bind ACT 34 in a specific manner, and that this occurs as interplay of all four zinc fingers. We also report that a sensitive kinetic balance, which is equilibrated by both zinc finger 1 and KTS, regulates the interaction with ACT 34. The stem-loop and the flanking nucleotides are important elements for specific recognition by WT 1 zinc fingers.},
  author       = {Nurmemmedov, Elmar and Kimbung, Raymond Yengo and Ladomery, Michael R and Thunnissen, Marjolein},
  issn         = {0003-9861},
  language     = {eng},
  pages        = {21--27},
  publisher    = {Academic Press},
  series       = {Archives of Biochemistry and Biophysics},
  title        = {Kinetic behaviour of WT 1's zinc finger domain in binding to the alpha-actinin-1 mRNA.},
  url          = {http://dx.doi.org/10.1016/j.abb.2010.02.013},
  volume       = {497},
  year         = {2010},
}