A common RNA recognition motif identified within a defined U1 RNA binding domain of the 70K U1 snRNP protein

Charles C. Query; Rex C. Bentley; Jack D. Keene

doi:10.1016/0092-8674(89)90175-X

A common RNA recognition motif identified within a defined U1 RNA binding domain of the 70K U1 snRNP protein

Charles C. Query, Rex C. Bentley, Jack D. Keene

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

524 Scopus citations

Abstract

We have defined the RNA binding domain of the 70K protein component of the U1 small nuclear ribonucleoprotein to a region of 111 amino acids. This domain encompasses an octamer sequence that has been observed in other proteins associated with RNA, but has not previously been shown to bind directly to a specific RNA sequence. Within the U1 RNA binding domain, an 80 amino acid consensus sequence that is conserved in many presumed RNA binding proteins was discerned. This sequence pattern appears to represent an RNA recognition motif (RRM) characteristic of a distinct family of proteins. By site-directed mutagenesis, we determined that the 70K protein consists of 437 amino acids (52 kd), and found that its aberrant electrophoretic migration is due to a carboxy-terminal charged domain structurally similar to two Drosophila proteins (su(w^a) and tra) that may regulate alternative pre-messenger RNA splicing.

Original language	English (US)
Pages (from-to)	89-101
Number of pages	13
Journal	Cell
Volume	57
Issue number	1
DOIs	https://doi.org/10.1016/0092-8674(89)90175-X
State	Published - Apr 7 1989
Externally published	Yes

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology

Access to Document

10.1016/0092-8674(89)90175-X

Cite this

@article{a187ff1acdd24f2db9cb521933697cbf,

title = "A common RNA recognition motif identified within a defined U1 RNA binding domain of the 70K U1 snRNP protein",

abstract = "We have defined the RNA binding domain of the 70K protein component of the U1 small nuclear ribonucleoprotein to a region of 111 amino acids. This domain encompasses an octamer sequence that has been observed in other proteins associated with RNA, but has not previously been shown to bind directly to a specific RNA sequence. Within the U1 RNA binding domain, an 80 amino acid consensus sequence that is conserved in many presumed RNA binding proteins was discerned. This sequence pattern appears to represent an RNA recognition motif (RRM) characteristic of a distinct family of proteins. By site-directed mutagenesis, we determined that the 70K protein consists of 437 amino acids (52 kd), and found that its aberrant electrophoretic migration is due to a carboxy-terminal charged domain structurally similar to two Drosophila proteins (su(wa) and tra) that may regulate alternative pre-messenger RNA splicing.",

author = "Query, {Charles C.} and Bentley, {Rex C.} and Keene, {Jack D.}",

note = "Funding Information: This paper is dedicated to Dr. Wolfgang K. Joklik for his contributions to virology as a scientist and a mentor. We thank Daniel Kenan for contributions to the alignment of RRM sequences, and Susan Deutscher for discussions of RNA-protein reconstitutions. This work was supported by grants from the Arthritis Foundation and the National Institutes of Health to J. D. K. C. C. Q. was supported by Medical Scientist Training Program grant GM 02121. R. C. 6. is the recipient of Physician Scientist Award Al 00909 from the National Institute of Allergy and Infectious Diseases. J. D. K. is a Pew Scholar in the Biomedical Sciences.",

year = "1989",

month = apr,

day = "7",

doi = "10.1016/0092-8674(89)90175-X",

language = "English (US)",

volume = "57",

pages = "89--101",

journal = "Cell",

issn = "0092-8674",

publisher = "Cell Press",

number = "1",

}

TY - JOUR

T1 - A common RNA recognition motif identified within a defined U1 RNA binding domain of the 70K U1 snRNP protein

AU - Query, Charles C.

AU - Bentley, Rex C.

AU - Keene, Jack D.

N1 - Funding Information: This paper is dedicated to Dr. Wolfgang K. Joklik for his contributions to virology as a scientist and a mentor. We thank Daniel Kenan for contributions to the alignment of RRM sequences, and Susan Deutscher for discussions of RNA-protein reconstitutions. This work was supported by grants from the Arthritis Foundation and the National Institutes of Health to J. D. K. C. C. Q. was supported by Medical Scientist Training Program grant GM 02121. R. C. 6. is the recipient of Physician Scientist Award Al 00909 from the National Institute of Allergy and Infectious Diseases. J. D. K. is a Pew Scholar in the Biomedical Sciences.

PY - 1989/4/7

Y1 - 1989/4/7

N2 - We have defined the RNA binding domain of the 70K protein component of the U1 small nuclear ribonucleoprotein to a region of 111 amino acids. This domain encompasses an octamer sequence that has been observed in other proteins associated with RNA, but has not previously been shown to bind directly to a specific RNA sequence. Within the U1 RNA binding domain, an 80 amino acid consensus sequence that is conserved in many presumed RNA binding proteins was discerned. This sequence pattern appears to represent an RNA recognition motif (RRM) characteristic of a distinct family of proteins. By site-directed mutagenesis, we determined that the 70K protein consists of 437 amino acids (52 kd), and found that its aberrant electrophoretic migration is due to a carboxy-terminal charged domain structurally similar to two Drosophila proteins (su(wa) and tra) that may regulate alternative pre-messenger RNA splicing.

AB - We have defined the RNA binding domain of the 70K protein component of the U1 small nuclear ribonucleoprotein to a region of 111 amino acids. This domain encompasses an octamer sequence that has been observed in other proteins associated with RNA, but has not previously been shown to bind directly to a specific RNA sequence. Within the U1 RNA binding domain, an 80 amino acid consensus sequence that is conserved in many presumed RNA binding proteins was discerned. This sequence pattern appears to represent an RNA recognition motif (RRM) characteristic of a distinct family of proteins. By site-directed mutagenesis, we determined that the 70K protein consists of 437 amino acids (52 kd), and found that its aberrant electrophoretic migration is due to a carboxy-terminal charged domain structurally similar to two Drosophila proteins (su(wa) and tra) that may regulate alternative pre-messenger RNA splicing.

UR - http://www.scopus.com/inward/record.url?scp=0024603237&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0024603237&partnerID=8YFLogxK

U2 - 10.1016/0092-8674(89)90175-X

DO - 10.1016/0092-8674(89)90175-X

M3 - Article

C2 - 2467746

AN - SCOPUS:0024603237

SN - 0092-8674

VL - 57

SP - 89

EP - 101

JO - Cell

JF - Cell

IS - 1

ER -

A common RNA recognition motif identified within a defined U1 RNA binding domain of the 70K U1 snRNP protein

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this