Identification and characterization of RED120: a conserved PWI domain protein with links to splicing and 3'-end formation

Puri Fortes; Dasa Longman; Susan McCracken; Joanna Y Ip; Raymond Poot; Iain W Mattaj; Javier F Cáceres; Benjamin J Blencowe

doi:10.1016/j.febslet.2007.05.066

Identification and characterization of RED120: a conserved PWI domain protein with links to splicing and 3'-end formation

Puri Fortes, Dasa Longman, Susan McCracken, Joanna Y Ip, Raymond Poot, Iain W Mattaj, Javier F Cáceres, Benjamin J Blencowe

Research output: Contribution to journal › Article › peer-review

Abstract / Description of output

Precursor (pre)-mRNA splicing can impact the efficiency of coupled steps in gene expression. SRm160 (SR-related nuclear matrix protein of 160 kDa), is a splicing coactivator that also functions as a 3'-end cleavage-stimulatory factor. Here, we have identified an evolutionary-conserved SRm160-interacting protein, referred to as hRED120 (for human Arg/Glu/Asp-rich protein of 120 kDa). hRED120 contains a conventional RNA recognition motif and, like SRm160, a PWI nucleic acid binding domain, suggesting that it has the potential to bridge different RNP complexes. Also, similar to SRm160, hRED120 associates with snRNP components, and remains associated with mRNA after splicing. Simultaneous suppression in Caenorhabditis elegans of the ortholog of hRED120 with the orthologs of splicing and 3'-end processing factors results in aberrant growth or developmental defects. These results suggest that RED120 may function to couple splicing with mRNA 3'-end formation.

Original language	English
Pages (from-to)	3087-97
Number of pages	11
Journal	FEBS Letters
Volume	581
Issue number	16
DOIs	https://doi.org/10.1016/j.febslet.2007.05.066
Publication status	Published - 26 Jun 2007

Keywords / Materials (for Non-textual outputs)

Amino Acid Sequence
Animals
Antigens, Nuclear
Caenorhabditis elegans
Cell Nucleus
Cloning, Molecular
Conserved Sequence
HeLa Cells
Humans
Molecular Sequence Data
Nuclear Matrix-Associated Proteins
Phylogeny
Protein Binding
Protein Structure, Tertiary
RNA 3' End Processing
RNA Precursors
RNA Splicing
RNA, Messenger
RNA-Binding Proteins
Sequence Homology, Amino Acid

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10.1016/j.febslet.2007.05.066

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title = "Identification and characterization of RED120: a conserved PWI domain protein with links to splicing and 3'-end formation",

abstract = "Precursor (pre)-mRNA splicing can impact the efficiency of coupled steps in gene expression. SRm160 (SR-related nuclear matrix protein of 160 kDa), is a splicing coactivator that also functions as a 3'-end cleavage-stimulatory factor. Here, we have identified an evolutionary-conserved SRm160-interacting protein, referred to as hRED120 (for human Arg/Glu/Asp-rich protein of 120 kDa). hRED120 contains a conventional RNA recognition motif and, like SRm160, a PWI nucleic acid binding domain, suggesting that it has the potential to bridge different RNP complexes. Also, similar to SRm160, hRED120 associates with snRNP components, and remains associated with mRNA after splicing. Simultaneous suppression in Caenorhabditis elegans of the ortholog of hRED120 with the orthologs of splicing and 3'-end processing factors results in aberrant growth or developmental defects. These results suggest that RED120 may function to couple splicing with mRNA 3'-end formation.",

keywords = "Amino Acid Sequence, Animals, Antigens, Nuclear, Caenorhabditis elegans, Cell Nucleus, Cloning, Molecular, Conserved Sequence, HeLa Cells, Humans, Molecular Sequence Data, Nuclear Matrix-Associated Proteins, Phylogeny, Protein Binding, Protein Structure, Tertiary, RNA 3' End Processing, RNA Precursors, RNA Splicing, RNA, Messenger, RNA-Binding Proteins, Sequence Homology, Amino Acid",

author = "Puri Fortes and Dasa Longman and Susan McCracken and Ip, {Joanna Y} and Raymond Poot and Mattaj, {Iain W} and C{\'a}ceres, {Javier F} and Blencowe, {Benjamin J}",

year = "2007",

month = jun,

day = "26",

doi = "10.1016/j.febslet.2007.05.066",

language = "English",

volume = "581",

pages = "3087--97",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Elsevier",

number = "16",

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TY - JOUR

T1 - Identification and characterization of RED120

T2 - a conserved PWI domain protein with links to splicing and 3'-end formation

AU - Fortes, Puri

AU - Longman, Dasa

AU - McCracken, Susan

AU - Ip, Joanna Y

AU - Poot, Raymond

AU - Mattaj, Iain W

AU - Cáceres, Javier F

AU - Blencowe, Benjamin J

PY - 2007/6/26

Y1 - 2007/6/26

N2 - Precursor (pre)-mRNA splicing can impact the efficiency of coupled steps in gene expression. SRm160 (SR-related nuclear matrix protein of 160 kDa), is a splicing coactivator that also functions as a 3'-end cleavage-stimulatory factor. Here, we have identified an evolutionary-conserved SRm160-interacting protein, referred to as hRED120 (for human Arg/Glu/Asp-rich protein of 120 kDa). hRED120 contains a conventional RNA recognition motif and, like SRm160, a PWI nucleic acid binding domain, suggesting that it has the potential to bridge different RNP complexes. Also, similar to SRm160, hRED120 associates with snRNP components, and remains associated with mRNA after splicing. Simultaneous suppression in Caenorhabditis elegans of the ortholog of hRED120 with the orthologs of splicing and 3'-end processing factors results in aberrant growth or developmental defects. These results suggest that RED120 may function to couple splicing with mRNA 3'-end formation.

AB - Precursor (pre)-mRNA splicing can impact the efficiency of coupled steps in gene expression. SRm160 (SR-related nuclear matrix protein of 160 kDa), is a splicing coactivator that also functions as a 3'-end cleavage-stimulatory factor. Here, we have identified an evolutionary-conserved SRm160-interacting protein, referred to as hRED120 (for human Arg/Glu/Asp-rich protein of 120 kDa). hRED120 contains a conventional RNA recognition motif and, like SRm160, a PWI nucleic acid binding domain, suggesting that it has the potential to bridge different RNP complexes. Also, similar to SRm160, hRED120 associates with snRNP components, and remains associated with mRNA after splicing. Simultaneous suppression in Caenorhabditis elegans of the ortholog of hRED120 with the orthologs of splicing and 3'-end processing factors results in aberrant growth or developmental defects. These results suggest that RED120 may function to couple splicing with mRNA 3'-end formation.

KW - Amino Acid Sequence

KW - Animals

KW - Antigens, Nuclear

KW - Caenorhabditis elegans

KW - Cell Nucleus

KW - Cloning, Molecular

KW - Conserved Sequence

KW - HeLa Cells

KW - Humans

KW - Molecular Sequence Data

KW - Nuclear Matrix-Associated Proteins

KW - Phylogeny

KW - Protein Binding

KW - Protein Structure, Tertiary

KW - RNA 3' End Processing

KW - RNA Precursors

KW - RNA Splicing

KW - RNA, Messenger

KW - RNA-Binding Proteins

KW - Sequence Homology, Amino Acid

U2 - 10.1016/j.febslet.2007.05.066

DO - 10.1016/j.febslet.2007.05.066

M3 - Article

C2 - 17560998

SN - 0014-5793

VL - 581

SP - 3087

EP - 3097

JO - FEBS Letters

JF - FEBS Letters

IS - 16

ER -

Identification and characterization of RED120: a conserved PWI domain protein with links to splicing and 3'-end formation

Abstract / Description of output

Keywords / Materials (for Non-textual outputs)

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