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 |