Purification of casein kinase I and isolation of cDNAs encoding multiple casein kinase I-like enzymes

Joie Rowles, Clive A. Slaughter, Carolyn Moomaw, Joan Hsu, Melanie H. Cobb

Research output: Contribution to journalArticle

112 Citations (Scopus)

Abstract

We have purified casein kinase I (CKI) over 6000-fold from bovine thymus and have sequenced seven tryptic peptides that account for nearly 25% of the primary sequence of the enzyme. By using PCR, partial cDNAs encoding CKI and a related enzyme (CKI-δ) were isolated. A product that may correspond to an alternatively spliced form of CKI was also detected. The CKI PCR product was used to probe a bovine brain cDNA library from which cDNAs corresponding to CKI (CKI-α) and two homologous enzymes (CKI-β and CKI-γ) were identified. The finding that there are at least four CKI-like enzymes suggests that CKI activity in tissues or cell extracts may be composed of multiple related but distinct protein kinases. This group of enzymes is not similar to any other known protein kinases and may, therefore, represent an additional branch of the protein kinase family.

Original languageEnglish (US)
Pages (from-to)9548-9552
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume88
Issue number21
DOIs
StatePublished - Jan 1 1991
Externally publishedYes

Fingerprint

Casein Kinase I
Complementary DNA
Enzymes
Protein Kinases
Polymerase Chain Reaction
Tissue Extracts
Cell Extracts
Gene Library
Thymus Gland

ASJC Scopus subject areas

  • General

Cite this

Purification of casein kinase I and isolation of cDNAs encoding multiple casein kinase I-like enzymes. / Rowles, Joie; Slaughter, Clive A.; Moomaw, Carolyn; Hsu, Joan; Cobb, Melanie H.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 88, No. 21, 01.01.1991, p. 9548-9552.

Research output: Contribution to journalArticle

@article{9d187ddd12964992b4ed364873ca80c0,
title = "Purification of casein kinase I and isolation of cDNAs encoding multiple casein kinase I-like enzymes",
abstract = "We have purified casein kinase I (CKI) over 6000-fold from bovine thymus and have sequenced seven tryptic peptides that account for nearly 25{\%} of the primary sequence of the enzyme. By using PCR, partial cDNAs encoding CKI and a related enzyme (CKI-δ) were isolated. A product that may correspond to an alternatively spliced form of CKI was also detected. The CKI PCR product was used to probe a bovine brain cDNA library from which cDNAs corresponding to CKI (CKI-α) and two homologous enzymes (CKI-β and CKI-γ) were identified. The finding that there are at least four CKI-like enzymes suggests that CKI activity in tissues or cell extracts may be composed of multiple related but distinct protein kinases. This group of enzymes is not similar to any other known protein kinases and may, therefore, represent an additional branch of the protein kinase family.",
author = "Joie Rowles and Slaughter, {Clive A.} and Carolyn Moomaw and Joan Hsu and Cobb, {Melanie H.}",
year = "1991",
month = "1",
day = "1",
doi = "10.1073/pnas.88.21.9548",
language = "English (US)",
volume = "88",
pages = "9548--9552",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "21",

}

TY - JOUR

T1 - Purification of casein kinase I and isolation of cDNAs encoding multiple casein kinase I-like enzymes

AU - Rowles, Joie

AU - Slaughter, Clive A.

AU - Moomaw, Carolyn

AU - Hsu, Joan

AU - Cobb, Melanie H.

PY - 1991/1/1

Y1 - 1991/1/1

N2 - We have purified casein kinase I (CKI) over 6000-fold from bovine thymus and have sequenced seven tryptic peptides that account for nearly 25% of the primary sequence of the enzyme. By using PCR, partial cDNAs encoding CKI and a related enzyme (CKI-δ) were isolated. A product that may correspond to an alternatively spliced form of CKI was also detected. The CKI PCR product was used to probe a bovine brain cDNA library from which cDNAs corresponding to CKI (CKI-α) and two homologous enzymes (CKI-β and CKI-γ) were identified. The finding that there are at least four CKI-like enzymes suggests that CKI activity in tissues or cell extracts may be composed of multiple related but distinct protein kinases. This group of enzymes is not similar to any other known protein kinases and may, therefore, represent an additional branch of the protein kinase family.

AB - We have purified casein kinase I (CKI) over 6000-fold from bovine thymus and have sequenced seven tryptic peptides that account for nearly 25% of the primary sequence of the enzyme. By using PCR, partial cDNAs encoding CKI and a related enzyme (CKI-δ) were isolated. A product that may correspond to an alternatively spliced form of CKI was also detected. The CKI PCR product was used to probe a bovine brain cDNA library from which cDNAs corresponding to CKI (CKI-α) and two homologous enzymes (CKI-β and CKI-γ) were identified. The finding that there are at least four CKI-like enzymes suggests that CKI activity in tissues or cell extracts may be composed of multiple related but distinct protein kinases. This group of enzymes is not similar to any other known protein kinases and may, therefore, represent an additional branch of the protein kinase family.

UR - http://www.scopus.com/inward/record.url?scp=0026093758&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026093758&partnerID=8YFLogxK

U2 - 10.1073/pnas.88.21.9548

DO - 10.1073/pnas.88.21.9548

M3 - Article

C2 - 1946367

AN - SCOPUS:0026093758

VL - 88

SP - 9548

EP - 9552

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 21

ER -