Imperial College London
Dr Enrique Martinez-Perez

DrEnriqueMartinez-Perez

Faculty of Medicine, Institute of Clinical Sciences

Reader in Chromosome Biology
 
 
 
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Contact

 

+44 (0)20 3313 4314enrique.martinez-perez Website

 
 
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Location

 

Hammersmith HospitalHammersmith Campus

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Summary

 

Publications

Citation

BibTex format

@article{Gao:2016:10.1101/gad.277350.116,
author = {Gao, J and Barroso, C and Zhang, P and Kim, H-M and Li, S and Labrador, L and Lightfoot, J and Gerashchenko, MV and Labunskyy, VM and Dong, M-Q and Martinez-Perez, E and Colaiacovo, MP},
doi = {10.1101/gad.277350.116},
journal = {Genes and Development},
pages = {2404--2416},
title = {N-terminal acetylation promotes synaptonemal complex assembly in C. elegans},
url = {http://dx.doi.org/10.1101/gad.277350.116},
volume = {30},
year = {2016}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - N-terminal acetylation of the first two amino acids on proteins is a prevalent cotranslational modification. Despite its abundance, the biological processes associated with this modification are not well understood. Here, we mapped the pattern of protein N-terminal acetylation in Caenorhabditis elegans, uncovering a conserved set of rules for this protein modification and identifying substrates for the N-terminal acetyltransferase B (NatB) complex. We observed an enrichment for global protein N-terminal acetylation and also specifically for NatB substrates in the nucleus, supporting the importance of this modification for regulating biological functions within this cellular compartment. Peptide profiling analysis provides evidence of cross-talk between N-terminal acetylation and internal modifications in a NAT substrate-specific manner. In vivo studies indicate that N-terminal acetylation is critical for meiosis, as it regulates the assembly of the synaptonemal complex (SC), a proteinaceous structure ubiquitously present during meiosis from yeast to humans. Specifically, N-terminal acetylation of NatB substrate SYP-1, an SC structural component, is critical for SC assembly. These findings provide novel insights into the biological functions of N-terminal acetylation and its essential role during meiosis.
AU  - Gao,J
AU  - Barroso,C
AU  - Zhang,P
AU  - Kim,H-M
AU  - Li,S
AU  - Labrador,L
AU  - Lightfoot,J
AU  - Gerashchenko,MV
AU  - Labunskyy,VM
AU  - Dong,M-Q
AU  - Martinez-Perez,E
AU  - Colaiacovo,MP
DO  - 10.1101/gad.277350.116
EP  - 2416
PY  - 2016///
SN  - 0890-9369
SP  - 2404
TI  - N-terminal acetylation promotes synaptonemal complex assembly in C. elegans
T2  - Genes and Development
UR  - http://dx.doi.org/10.1101/gad.277350.116
UR  - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000388810500006&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR  - http://genesdev.cshlp.org/content/30/21/2404
VL  - 30
ER  -
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