PMID- 36094910
OWN - NLM
STAT- MEDLINE
DCOM- 20220914
LR  - 20230607
IS  - 1932-6203 (Electronic)
IS  - 1932-6203 (Linking)
VI  - 17
IP  - 9
DP  - 2022
TI  - The PCI domains are "winged" HEAT domains.
PG  - e0268664
LID - 10.1371/journal.pone.0268664 [doi]
LID - e0268664
AB  - The HEAT domains are a family of helical hairpin repeat domains, composed of four 
      or more hairpins. HEAT is derived from the names of four family members: 
      huntingtin, eukaryotic translation elongation factor 3 (eEF3), protein 
      phosphatase 2 regulatory A subunit (PP2A), and mechanistic target of rapamycin 
      (mTOR). HEAT domain-containing proteins play roles in a wide range of cellular 
      processes, such as protein synthesis, nuclear transport and metabolism, and cell 
      signaling. The PCI domains are a related group of helical hairpin domains, with a 
      "winged-helix" (WH) subdomain at their C-terminus, which is responsible for 
      multi-subunit complex formation with other PCI domains. The name is derived from 
      the complexes, where these domains are found: the 26S Proteasome "lid" regulatory 
      subcomplex, the COP9 signalosome (CSN), and eukaryotic translation initiation 
      factor 3 (eIF3). We noted that in structure similarity searches using HEAT 
      domains, sometimes PCI domains appeared in the search results ahead of other HEAT 
      domains, which indicated that the PCI domains could be members of the HEAT domain 
      family, and not a related but separate group, as currently thought. Here, we 
      report extensive structure similarity analysis of HEAT and PCI domains, both 
      within and between the two groups of proteins. We present evidence that the PCI 
      domains as a group have greater structural similarity with individual groups of 
      HEAT domains than some of the HEAT domain groups have among each other. 
      Therefore, our results indicate that the PCI domains have evolved from a HEAT 
      domain that acquired a WH subdomain. The WH subdomain in turn mediated 
      self-association into a multi-subunit complex, which eventually evolved into the 
      common ancestor of the Proteasome lid/CSN/eIF3.
FAU - Paul, Eleanor Elise
AU  - Paul EE
AUID- ORCID: 0000-0002-8937-795X
AD  - Department of Physiology & Biophysics, Boston University School of Medicine, 
      Boston, Massachusetts, United States of America.
FAU - Marintchev, Assen
AU  - Marintchev A
AUID- ORCID: 0000-0002-9901-3500
AD  - Department of Physiology & Biophysics, Boston University School of Medicine, 
      Boston, Massachusetts, United States of America.
LA  - eng
GR  - R01 GM134113/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
DEP - 20220912
PL  - United States
TA  - PLoS One
JT  - PloS one
JID - 101285081
RN  - 0 (Eukaryotic Initiation Factor-3)
RN  - 0 (Proteins)
RN  - EC 3.4.19.12 (COP9 Signalosome Complex)
SB  - IM
MH  - COP9 Signalosome Complex
MH  - *Eukaryotic Initiation Factor-3/chemistry
MH  - Hot Temperature
MH  - *Percutaneous Coronary Intervention
MH  - Proteins
PMC - PMC9467303
COIS- The authors have declared that no competing interests exist.
EDAT- 2022/09/13 06:00
MHDA- 2022/09/15 06:00
PMCR- 2022/09/12
CRDT- 2022/09/12 13:32
PHST- 2022/05/02 00:00 [received]
PHST- 2022/08/17 00:00 [accepted]
PHST- 2022/09/12 13:32 [entrez]
PHST- 2022/09/13 06:00 [pubmed]
PHST- 2022/09/15 06:00 [medline]
PHST- 2022/09/12 00:00 [pmc-release]
AID - PONE-D-22-12899 [pii]
AID - 10.1371/journal.pone.0268664 [doi]
PST - epublish
SO  - PLoS One. 2022 Sep 12;17(9):e0268664. doi: 10.1371/journal.pone.0268664. 
      eCollection 2022.