Knowledge Center Catalog

Genome-scale analysis of regulatory protein acetylation enzymes from photosynthetic eukaryotes (Record no. 64767)

MARC details
000 -LEADER
fixed length control field 03764nab a22003497a 4500
001 - CONTROL NUMBER
control field 64767
003 - CONTROL NUMBER IDENTIFIER
control field MX-TxCIM
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20220103145041.0
008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION
fixed length control field 210625s2017 xxk|||p|op||| 00| 0 eng d
022 ## - INTERNATIONAL STANDARD SERIAL NUMBER
International Standard Serial Number 1471-2164
024 8# - OTHER STANDARD IDENTIFIER
Standard number or code https://doi.org/10.1186/s12864-017-3894-0
040 ## - CATALOGING SOURCE
Original cataloging agency MX-TxCIM
041 ## - LANGUAGE CODE
Language code of text/sound track or separate title eng
100 1# - MAIN ENTRY--PERSONAL NAME
9 (RLIN) 26205
Personal name Uhrig, R.G.
245 10 - TITLE STATEMENT
Title Genome-scale analysis of regulatory protein acetylation enzymes from photosynthetic eukaryotes
260 ## - PUBLICATION, DISTRIBUTION, ETC. (IMPRINT)
Place of publication, distribution, etc. London (United Kingdom) :
Name of publisher, distributor, etc. BioMed Central,
Date of publication, distribution, etc. 2017.
500 ## - GENERAL NOTE
General note Peer review
500 ## - GENERAL NOTE
General note Open Access
520 ## - SUMMARY, ETC.
Summary, etc. Background: Reversible protein acetylation occurring on Lys-Ne has emerged as a key regulatory post-translational modification in eukaryotes. It is mediated by two groups of enzymes: lysine acetyltransferases (KATs) and lysine deacetylases (KDACs) that catalyze the addition and removal of acetyl groups from target proteins. Estimates indicate that protein acetylation is second to protein phosphorylation in abundance, with thousands of acetylated sites now identified in different subcellular compartments. Considering the important regulatory role of protein phosphorylation, elucidating the diversity of KATs and KDACs across photosynthetic eukaryotes is essential in furthering our understanding of the impact of reversible protein acetylation on plant cell processes. Results: We report a genome-scale analysis of lysine acetyltransferase (KAT)- and lysine deacetylase (KDAC)-families from 53 photosynthetic eukaryotes. KAT and KDAC orthologs were identified in sequenced genomes ranging from glaucophytes and algae to land plants and then analyzed for evolutionary relationships. Based on consensus molecular phylogenetic and subcellular localization data we found new sub-classes of enzymes in established KAT- and KDAC-families. Specifically, we identified a non-photosynthetic origin of the HD-tuin family KDACs, a new monocot-specific Class I HDA-family sub-class, and a phylogenetically distinct Class II algal/heterokont sub-class which maintains an ankyrin domain not conserved in land plant Class II KDACs. Protein structure analysis showed that HDA- and SRT-KDACs exist as bare catalytic subunits with highly conserved median protein length, while all KATs maintained auxiliary domains, with CBP- and TAFII250-KATs displaying protein domain gain and loss over the course of photosynthetic eukaryote evolution in addition to variable protein length. Lastly, promoter element enrichment analyses across species revealed conserved cis-regulatory sequences that support KAT and KDAC involvement in the regulation of plant development, cold/drought stress response, as well as cellular processes such as the circadian clock. Conclusions: Our results reveal new evolutionary, structural, and biological insights into the KAT- and KDAC-families of photosynthetic eukaryotes, including evolutionary parallels to protein kinases and protein phosphatases. Further, we provide a comprehensive annotation framework through our extensive phylogenetic analysis, from which future research investigating aspects of protein acetylation in plants can use to position new findings in a broader context.
546 ## - LANGUAGE NOTE
Language note Text in English
650 #7 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Acetylation
9 (RLIN) 16334
Source of heading or term AGROVOC
650 #7 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Eukaryota
9 (RLIN) 25734
Source of heading or term AGROVOC
650 #7 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Lysine
9 (RLIN) 5257
Source of heading or term AGROVOC
650 #7 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Genomics
9 (RLIN) 1132
Source of heading or term AGROVOC
700 1# - ADDED ENTRY--PERSONAL NAME
9 (RLIN) 4656
Personal name Schlapfer, P.
700 1# - ADDED ENTRY--PERSONAL NAME
9 (RLIN) 26206
Personal name Mehta, D.
700 1# - ADDED ENTRY--PERSONAL NAME
9 (RLIN) 26207
Personal name Hirsch-Hoffmann, M.
700 1# - ADDED ENTRY--PERSONAL NAME
9 (RLIN) 26208
Personal name Gruissem, W.
773 0# - HOST ITEM ENTRY
Record control number 56896
International Standard Serial Number 1471-2164
Place, publisher, and date of publication London (United Kingdom) : BioMed Central, 2017.
Title BMC Genomics
Related parts v. 18, art. 514
856 4# - ELECTRONIC LOCATION AND ACCESS
Link text Click here to access online
Uniform Resource Identifier https://doi.org/10.1186/s12864-017-3894-0
942 ## - ADDED ENTRY ELEMENTS (KOHA)
Source of classification or shelving scheme Dewey Decimal Classification
Koha item type Article
Suppress in OPAC No
Holdings
Date last seen Total Checkouts Price effective from Koha item type Lost status Source of classification or shelving scheme Damaged status Not for loan Collection code Withdrawn status Home library Current library Date acquired
12/20/2021   12/20/2021 Article Not Lost Dewey Decimal Classification     Reprints Collection   CIMMYT Knowledge Center: John Woolston Library CIMMYT Knowledge Center: John Woolston Library 12/20/2021

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