Lysine Acetylation Controls Local Protein Conformation by Influencing Proline Isomerization

Lysine Acetylation Controls Local Protein Conformation by Influencing Proline Isomerization

Gene transcription responds to stress and metabolic signals to optimize growth and survival. Histone H3 (H3) lysine 4 trimethylation (K4me3) facilitates state changes, but how levels are coordinated with the environment is unclear. Here, we show that isomerization of H3 at the alanine 15-proline 16...

Full description

Bibliographic Details
Main Authors: Howe, Françoise S., Boubriak, Ivan, Sale, Matthew J., Nair, Anitha, Clynes, David, Grijzenhout, Anne, Murray, Struan C., Woloszczuk, Ronja, Mellor, Jane
Format: Online
Language:English
Published: Cell Press 2014
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4157579/
id pubmed-4157579
recordtype oai_dc
spelling pubmed-41575792014-09-09 Lysine Acetylation Controls Local Protein Conformation by Influencing Proline Isomerization Howe, Françoise S. Boubriak, Ivan Sale, Matthew J. Nair, Anitha Clynes, David Grijzenhout, Anne Murray, Struan C. Woloszczuk, Ronja Mellor, Jane Article Gene transcription responds to stress and metabolic signals to optimize growth and survival. Histone H3 (H3) lysine 4 trimethylation (K4me3) facilitates state changes, but how levels are coordinated with the environment is unclear. Here, we show that isomerization of H3 at the alanine 15-proline 16 (A15-P16) peptide bond is influenced by lysine 14 (K14) and controls gene-specific K4me3 by balancing the actions of Jhd2, the K4me3 demethylase, and Spp1, a subunit of the Set1 K4 methyltransferase complex. Acetylation at K14 favors the A15-P16trans conformation and reduces K4me3. Environmental stress-induced genes are most sensitive to the changes at K14 influencing H3 tail conformation and K4me3. By contrast, ribosomal protein genes maintain K4me3, required for their repression during stress, independently of Spp1, K14, and P16. Thus, the plasticity in control of K4me3, via signaling to K14 and isomerization at P16, informs distinct gene regulatory mechanisms and processes involving K4me3. Cell Press 2014-09-04 /pmc/articles/PMC4157579/ /pubmed/25127513 http://dx.doi.org/10.1016/j.molcel.2014.07.004 Text en © 2014 The Authors
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Howe, Françoise S.
Boubriak, Ivan
Sale, Matthew J.
Nair, Anitha
Clynes, David
Grijzenhout, Anne
Murray, Struan C.
Woloszczuk, Ronja
Mellor, Jane
spellingShingle Howe, Françoise S.
Boubriak, Ivan
Sale, Matthew J.
Nair, Anitha
Clynes, David
Grijzenhout, Anne
Murray, Struan C.
Woloszczuk, Ronja
Mellor, Jane
Lysine Acetylation Controls Local Protein Conformation by Influencing Proline Isomerization
author_facet Howe, Françoise S.
Boubriak, Ivan
Sale, Matthew J.
Nair, Anitha
Clynes, David
Grijzenhout, Anne
Murray, Struan C.
Woloszczuk, Ronja
Mellor, Jane
author_sort Howe, Françoise S.
title Lysine Acetylation Controls Local Protein Conformation by Influencing Proline Isomerization
title_short Lysine Acetylation Controls Local Protein Conformation by Influencing Proline Isomerization
title_full Lysine Acetylation Controls Local Protein Conformation by Influencing Proline Isomerization
title_fullStr Lysine Acetylation Controls Local Protein Conformation by Influencing Proline Isomerization
title_full_unstemmed Lysine Acetylation Controls Local Protein Conformation by Influencing Proline Isomerization
title_sort lysine acetylation controls local protein conformation by influencing proline isomerization
description Gene transcription responds to stress and metabolic signals to optimize growth and survival. Histone H3 (H3) lysine 4 trimethylation (K4me3) facilitates state changes, but how levels are coordinated with the environment is unclear. Here, we show that isomerization of H3 at the alanine 15-proline 16 (A15-P16) peptide bond is influenced by lysine 14 (K14) and controls gene-specific K4me3 by balancing the actions of Jhd2, the K4me3 demethylase, and Spp1, a subunit of the Set1 K4 methyltransferase complex. Acetylation at K14 favors the A15-P16trans conformation and reduces K4me3. Environmental stress-induced genes are most sensitive to the changes at K14 influencing H3 tail conformation and K4me3. By contrast, ribosomal protein genes maintain K4me3, required for their repression during stress, independently of Spp1, K14, and P16. Thus, the plasticity in control of K4me3, via signaling to K14 and isomerization at P16, informs distinct gene regulatory mechanisms and processes involving K4me3.
publisher Cell Press
publishDate 2014
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4157579/
_version_ 1613131890596773888

Similar Items