Nuclear transport and phosphorylation of the RNA binding Xenopus zinc finger protein XFG 5-1

I van Wijk, J Burfeind, T Pieler

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

XFG 5-1 is a Krüppel-type Xenopus zinc finger protein with specific RNA homopolymer binding activity in vitro. In the oocyte, the protein is distributed between nucleus and cytoplasm; the nuclear fraction, not the cytoplasm, contains phosphorylated isoform(s) of XFG 5-1. In vitro phosphorylation by use of oocyte/egg extracts or purified casein kinase II is specific to the amino-terminal portion of the protein. The carboxy-terminal zinc finger domain contains a signal sufficient for nuclear transport. Overexpression of either full length XFG 5-1 or of the carboxy-terminal portion alone, which maintains RNA binding and nuclear import activities, was achieved in Xenopus embryos by mRNA injection. This treatment did not result in impaired regulation of development, suggesting that XFG 5-1 functions in a way distinct from the mode of action exemplified in the Drosophila zinc finger protein Krüppel.

Original languageEnglish
Pages (from-to)63-72
Number of pages10
JournalMechanisms of development
Volume39
Issue number1-2
Publication statusPublished - Nov 1992

Cite this

@article{3fe6cea0dbb743c2a0212904ad1a95c4,
title = "Nuclear transport and phosphorylation of the RNA binding Xenopus zinc finger protein XFG 5-1",
abstract = "XFG 5-1 is a Kr{\"u}ppel-type Xenopus zinc finger protein with specific RNA homopolymer binding activity in vitro. In the oocyte, the protein is distributed between nucleus and cytoplasm; the nuclear fraction, not the cytoplasm, contains phosphorylated isoform(s) of XFG 5-1. In vitro phosphorylation by use of oocyte/egg extracts or purified casein kinase II is specific to the amino-terminal portion of the protein. The carboxy-terminal zinc finger domain contains a signal sufficient for nuclear transport. Overexpression of either full length XFG 5-1 or of the carboxy-terminal portion alone, which maintains RNA binding and nuclear import activities, was achieved in Xenopus embryos by mRNA injection. This treatment did not result in impaired regulation of development, suggesting that XFG 5-1 functions in a way distinct from the mode of action exemplified in the Drosophila zinc finger protein Kr{\"u}ppel.",
keywords = "Amino Acid Sequence, Animals, Biological Transport, Cell Nucleus/metabolism, Embryonic and Fetal Development/genetics, Microinjections, Molecular Sequence Data, Phosphorylation, Protein Processing, Post-Translational, Protein Sorting Signals/physiology, RNA-Binding Proteins/genetics, Recombinant Fusion Proteins/metabolism, Xenopus Proteins, Xenopus laevis/embryology, Zinc Fingers/genetics",
author = "{van Wijk}, I and J Burfeind and T Pieler",
year = "1992",
month = "11",
language = "English",
volume = "39",
pages = "63--72",
journal = "Mechanisms of development",
issn = "0925-4773",
publisher = "Elsevier Ireland Ltd",
number = "1-2",

}

Nuclear transport and phosphorylation of the RNA binding Xenopus zinc finger protein XFG 5-1. / van Wijk, I; Burfeind, J; Pieler, T.

In: Mechanisms of development, Vol. 39, No. 1-2, 11.1992, p. 63-72.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Nuclear transport and phosphorylation of the RNA binding Xenopus zinc finger protein XFG 5-1

AU - van Wijk, I

AU - Burfeind, J

AU - Pieler, T

PY - 1992/11

Y1 - 1992/11

N2 - XFG 5-1 is a Krüppel-type Xenopus zinc finger protein with specific RNA homopolymer binding activity in vitro. In the oocyte, the protein is distributed between nucleus and cytoplasm; the nuclear fraction, not the cytoplasm, contains phosphorylated isoform(s) of XFG 5-1. In vitro phosphorylation by use of oocyte/egg extracts or purified casein kinase II is specific to the amino-terminal portion of the protein. The carboxy-terminal zinc finger domain contains a signal sufficient for nuclear transport. Overexpression of either full length XFG 5-1 or of the carboxy-terminal portion alone, which maintains RNA binding and nuclear import activities, was achieved in Xenopus embryos by mRNA injection. This treatment did not result in impaired regulation of development, suggesting that XFG 5-1 functions in a way distinct from the mode of action exemplified in the Drosophila zinc finger protein Krüppel.

AB - XFG 5-1 is a Krüppel-type Xenopus zinc finger protein with specific RNA homopolymer binding activity in vitro. In the oocyte, the protein is distributed between nucleus and cytoplasm; the nuclear fraction, not the cytoplasm, contains phosphorylated isoform(s) of XFG 5-1. In vitro phosphorylation by use of oocyte/egg extracts or purified casein kinase II is specific to the amino-terminal portion of the protein. The carboxy-terminal zinc finger domain contains a signal sufficient for nuclear transport. Overexpression of either full length XFG 5-1 or of the carboxy-terminal portion alone, which maintains RNA binding and nuclear import activities, was achieved in Xenopus embryos by mRNA injection. This treatment did not result in impaired regulation of development, suggesting that XFG 5-1 functions in a way distinct from the mode of action exemplified in the Drosophila zinc finger protein Krüppel.

KW - Amino Acid Sequence

KW - Animals

KW - Biological Transport

KW - Cell Nucleus/metabolism

KW - Embryonic and Fetal Development/genetics

KW - Microinjections

KW - Molecular Sequence Data

KW - Phosphorylation

KW - Protein Processing, Post-Translational

KW - Protein Sorting Signals/physiology

KW - RNA-Binding Proteins/genetics

KW - Recombinant Fusion Proteins/metabolism

KW - Xenopus Proteins

KW - Xenopus laevis/embryology

KW - Zinc Fingers/genetics

M3 - Article

VL - 39

SP - 63

EP - 72

JO - Mechanisms of development

JF - Mechanisms of development

SN - 0925-4773

IS - 1-2

ER -