Literature DB >> 9178570

Zinc finger-like motif conserved in a family of RNA binding proteins.

Y Matsushima1, K Matsumura, Y Kitagawa.   

Abstract

NP220s compose a family of RNA binding proteins together with matrin 3, one of major proteins of the nuclear matrix. They have repeats of RNA recognition motif (RRM; MH2) homologous to RRM in heterogeneous nuclear RNPs I/L in addition to MH1 and MH3 with unknown function. In search of additional homologous sequences, we found the reported sequence of rat matrin 3 is partially incorrect. Correction of this sequence showed that the NP220 family has a fourth homologous motif with the characteristics of a Cys2-His2 zinc finger-like motif. The sequence of this motif is perfectly conserved in human and mouse NP220s despite their 75% overall sequence homology.

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Year:  1997        PMID: 9178570     DOI: 10.1271/bbb.61.905

Source DB:  PubMed          Journal:  Biosci Biotechnol Biochem        ISSN: 0916-8451            Impact factor:   2.043


  5 in total

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Journal:  Genes Dev       Date:  1999-09-15       Impact factor: 11.361

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Authors:  E Lalli; K Ohe; C Hindelang; P Sassone-Corsi
Journal:  Mol Cell Biol       Date:  2000-07       Impact factor: 4.272

4.  The cohesin complex: sequence homologies, interaction networks and shared motifs.

Authors:  S Jones; J Sgouros
Journal:  Genome Biol       Date:  2001-03-06       Impact factor: 13.583

5.  Domain function and predicted structure of three heterodimeric endonuclease subunits of RNA editing catalytic complexes in Trypanosoma brucei.

Authors:  Jason Carnes; Suzanne M McDermott; Isaac Lewis; Maxwell Tracy; Kenneth Stuart
Journal:  Nucleic Acids Res       Date:  2022-09-23       Impact factor: 19.160

  5 in total

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