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Tetratrico peptide repeat interactions: to TPR or not to TPR?

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Lamb, John R, Tugendreich, Stuart, Hieter, Phil·1995·Trends in Biochemical Sciences
DOI 10.1016/s0968-0004(00)89037-4
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Abstract

Tetratrico peptide repeat interactions: to T?R or not to TPR?The tetratrico peptide repeat (TPR) is a degenerate 34-amino acid repeated motif that is widespread in evolutionL TPR proteins have been discovered in organisms as diverse as bacteria and humans, and in a variety of subcellular locations, including the nucleus, the cytoplasm and mitochondria.Processes involving TPR proteins include cellcycle control, transcription repression, stress response, protein kinase inhibition, mitochondrial and peroxisomal protein transport and neurogenesisL Therefore, there appears to be no common biochemical function connecting TPR-containing proteins.TPRs are frequently tandemly arrayed, although it is also common for single or double TPRs to be found separated from the arrays (Fig. In).Comparison of TPRs from a variety of proteins reveals eight loosely conserved consensus residues (-W-LG-Y-A-F-A-P-; see Fig. 2a and Refs 2, 3) within the 34 amino acids that define the motif.These residues are conserved in terms of their size, hydrophobicity and spacing.The high degree of sequence diversity observed in TPRs is consistent with the diversity of function o[ TPR-containing proteins.TPR-TPR intsractions Overall, TPRs have a high probability of forming amphipathic a-helices 2,3 in two domains, A and B. Detailed secondary structure predictions have been made whereby domain A OV-LG-Y) forms a hydrophobic pocket into which the bulky phenylalanine sidechain of domain B (A-F-A) fits (the so-called knob and hole model 2, see Fig. lb).The prediction of this model is that TPRs interact with each other and therefor mediatc protein-protein interactions.These interactions could form intraand/or intermolecular contacts between protein segments.Evidence for direct TPR-TPR-mediated protein-protein interactions has not emerged, although some TPR-containing proteins, such as CDC16, CDC23 and CDC27 (Ref.4), have

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  • The proposed role for the TPRs would be consistent with their high conservation across species and the fact that TPRs are involved in protein-protein interactions.

    “The proposed role for the TPRs would be consistent with their high conservation across species (Gindhart and Goldstein, 1996), and the fact that TPRs are involved in protein–protein interactions (Lamb et al., 1995; Das et al., 1998).”

    From Light Chain– dependent Regulation of Kinesin's Interaction with Microtubules (1998) · cites this paper as Lamb et al., 1995

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Authors
Lamb, J. R., Tugendreich, S., & Hieter, P.
Affiliations
Johns Hopkins University (US)
ORCID
Venue
Trends in Biochemical Sciences
Publisher
Elsevier BV
Published
1995-07
Volume
20
Issue
7
Pages
257-259
ISSN
0968-0004 (ISSN-L)
DOI
10.1016/s0968-0004(00)89037-4
OpenAlex
W2038186997
Cited by
626
References
19
Citations by year
2026: 5 · 2025: 2 · 2024: 10 · 2023: 9 · 2022: 7 · 2021: 17 · 2020: 14 · 2019: 10 · 2018: 5 · 2017: 18 · 2016: 11 · 2015: 6 · 2014: 15 · 2013: 8 · 2012: 17
FWCI
2.22
Type
journal article
Language
en
Open access
Licence
Locations
  • Trends in Biochemical Sciences (publishedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
Keywords
TPR proteins, protein-protein interaction, amphipathic helix, CDC16, CDC23, CDC27, mitochondrial protein transport, transcriptional repression, cell cycle regulation
MeSH terms
Amino Acid Sequence, Biological Evolution, Models, Molecular, Molecular Sequence Data, Peptides, Consensus Sequence, Conserved Sequence, Sequence Homology, Amino Acid, Protein Structure, Secondary

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