The α-subunit of protein prenyltransferases is a member of the tetratricopeptide repeat family

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

Lipidation catalyzed by protein prenyltransferases is essential for the biological function of a number of eukaryotic proteins, many of which are involved in signal transduction and vesicular traffic regulation. Sequence similarity searches reveal that the α-subunit of protein prenyltransferases (PTα) is a member of the tetratricopeptide repeat (TPR) superfamily. This finding makes the three-dimensional structure of the rat protein farnesyltransferase the first structural model of a TPR protein interacting with its protein partner. Structural comparison of the two TPR domains in protein farnesyltransferase and protein phosphatase 5 indicates that variation in TPR consensus residues may affect protein binding specificity through altering the overall shape of the TPR superhelix. A general approach to evolutionary analysis of proteins with repetitive sequence motifs has been developed and applied to the protein prenyltransferases and other TPR proteins. The results suggest that all members in PTα family originated from a common multirepeat ancestor, while the common ancestor of PTα and other members of TPR superfamily is likely to be a single repeat protein.

Original languageEnglish (US)
Pages (from-to)1658-1667
Number of pages10
JournalProtein Science
Volume8
Issue number8
StatePublished - 1999

Fingerprint

Dimethylallyltranstransferase
Protein Subunits
Proteins
Signal transduction
Nucleic Acid Repetitive Sequences
Structural Models
Protein Binding
Rats
Signal Transduction

Keywords

  • Helix packing
  • Protein evolution
  • Protein prenyltransferases
  • Protein-protein interactions
  • Tetratricopeptide repeat

ASJC Scopus subject areas

  • Biochemistry

Cite this

The α-subunit of protein prenyltransferases is a member of the tetratricopeptide repeat family. / Zhang, Hong; Grishin, Nick V.

In: Protein Science, Vol. 8, No. 8, 1999, p. 1658-1667.

Research output: Contribution to journalArticle

@article{4abffeed2c264fff927e98bf5dfec115,
title = "The α-subunit of protein prenyltransferases is a member of the tetratricopeptide repeat family",
abstract = "Lipidation catalyzed by protein prenyltransferases is essential for the biological function of a number of eukaryotic proteins, many of which are involved in signal transduction and vesicular traffic regulation. Sequence similarity searches reveal that the α-subunit of protein prenyltransferases (PTα) is a member of the tetratricopeptide repeat (TPR) superfamily. This finding makes the three-dimensional structure of the rat protein farnesyltransferase the first structural model of a TPR protein interacting with its protein partner. Structural comparison of the two TPR domains in protein farnesyltransferase and protein phosphatase 5 indicates that variation in TPR consensus residues may affect protein binding specificity through altering the overall shape of the TPR superhelix. A general approach to evolutionary analysis of proteins with repetitive sequence motifs has been developed and applied to the protein prenyltransferases and other TPR proteins. The results suggest that all members in PTα family originated from a common multirepeat ancestor, while the common ancestor of PTα and other members of TPR superfamily is likely to be a single repeat protein.",
keywords = "Helix packing, Protein evolution, Protein prenyltransferases, Protein-protein interactions, Tetratricopeptide repeat",
author = "Hong Zhang and Grishin, {Nick V.}",
year = "1999",
language = "English (US)",
volume = "8",
pages = "1658--1667",
journal = "Protein Science",
issn = "0961-8368",
publisher = "Cold Spring Harbor Laboratory Press",
number = "8",

}

TY - JOUR

T1 - The α-subunit of protein prenyltransferases is a member of the tetratricopeptide repeat family

AU - Zhang, Hong

AU - Grishin, Nick V.

PY - 1999

Y1 - 1999

N2 - Lipidation catalyzed by protein prenyltransferases is essential for the biological function of a number of eukaryotic proteins, many of which are involved in signal transduction and vesicular traffic regulation. Sequence similarity searches reveal that the α-subunit of protein prenyltransferases (PTα) is a member of the tetratricopeptide repeat (TPR) superfamily. This finding makes the three-dimensional structure of the rat protein farnesyltransferase the first structural model of a TPR protein interacting with its protein partner. Structural comparison of the two TPR domains in protein farnesyltransferase and protein phosphatase 5 indicates that variation in TPR consensus residues may affect protein binding specificity through altering the overall shape of the TPR superhelix. A general approach to evolutionary analysis of proteins with repetitive sequence motifs has been developed and applied to the protein prenyltransferases and other TPR proteins. The results suggest that all members in PTα family originated from a common multirepeat ancestor, while the common ancestor of PTα and other members of TPR superfamily is likely to be a single repeat protein.

AB - Lipidation catalyzed by protein prenyltransferases is essential for the biological function of a number of eukaryotic proteins, many of which are involved in signal transduction and vesicular traffic regulation. Sequence similarity searches reveal that the α-subunit of protein prenyltransferases (PTα) is a member of the tetratricopeptide repeat (TPR) superfamily. This finding makes the three-dimensional structure of the rat protein farnesyltransferase the first structural model of a TPR protein interacting with its protein partner. Structural comparison of the two TPR domains in protein farnesyltransferase and protein phosphatase 5 indicates that variation in TPR consensus residues may affect protein binding specificity through altering the overall shape of the TPR superhelix. A general approach to evolutionary analysis of proteins with repetitive sequence motifs has been developed and applied to the protein prenyltransferases and other TPR proteins. The results suggest that all members in PTα family originated from a common multirepeat ancestor, while the common ancestor of PTα and other members of TPR superfamily is likely to be a single repeat protein.

KW - Helix packing

KW - Protein evolution

KW - Protein prenyltransferases

KW - Protein-protein interactions

KW - Tetratricopeptide repeat

UR - http://www.scopus.com/inward/record.url?scp=0032807382&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032807382&partnerID=8YFLogxK

M3 - Article

VL - 8

SP - 1658

EP - 1667

JO - Protein Science

JF - Protein Science

SN - 0961-8368

IS - 8

ER -