Heterozygous yeast deletion collection screens reveal essential targets of Hsp90.
Hsp90 is an essential eukaryotic chaperone with a role in folding specific "client" proteins such as kinases and hormone receptors. Previously performed homozygous diploid yeast deletion collection screens uncovered broad requirements for Hsp90 in cellular transport and cell cycle progress...
| Main Authors: | , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2011-01-01
|
| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3227642?pdf=render |
| _version_ | 1819074339318792192 |
|---|---|
| author | Eric A Franzosa Véronique Albanèse Judith Frydman Yu Xia Amie J McClellan |
| author_facet | Eric A Franzosa Véronique Albanèse Judith Frydman Yu Xia Amie J McClellan |
| author_sort | Eric A Franzosa |
| collection | DOAJ |
| description | Hsp90 is an essential eukaryotic chaperone with a role in folding specific "client" proteins such as kinases and hormone receptors. Previously performed homozygous diploid yeast deletion collection screens uncovered broad requirements for Hsp90 in cellular transport and cell cycle progression. These screens also revealed that the requisite cellular functions of Hsp90 change with growth temperature. We present here for the first time the results of heterozygous deletion collection screens conducted at the hypothermic stress temperature of 15°C. Extensive bioinformatic analyses were performed on the resulting data in combination with data from homozygous and heterozygous screens previously conducted at normal (30°C) and hyperthermic stress (37°C) growth temperatures. Our resulting meta-analysis uncovered extensive connections between Hsp90 and (1) general transcription, (2) ribosome biogenesis and (3) GTP binding proteins. Predictions from bioinformatic analyses were tested experimentally, supporting a role for Hsp90 in ribosome stability. Importantly, the integrated analysis of the 15°C heterozygous deletion pool screen with previously conducted 30°C and 37°C screens allows for essential genetic targets of Hsp90 to emerge. Altogether, these novel contributions enable a more complete picture of essential Hsp90 functions. |
| first_indexed | 2024-12-21T18:07:57Z |
| format | Article |
| id | doaj.art-b32461596c464d379d253e436a18d3a6 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-21T18:07:57Z |
| publishDate | 2011-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-b32461596c464d379d253e436a18d3a62022-12-21T18:54:52ZengPublic Library of Science (PLoS)PLoS ONE1932-62032011-01-01611e2821110.1371/journal.pone.0028211Heterozygous yeast deletion collection screens reveal essential targets of Hsp90.Eric A FranzosaVéronique AlbanèseJudith FrydmanYu XiaAmie J McClellanHsp90 is an essential eukaryotic chaperone with a role in folding specific "client" proteins such as kinases and hormone receptors. Previously performed homozygous diploid yeast deletion collection screens uncovered broad requirements for Hsp90 in cellular transport and cell cycle progression. These screens also revealed that the requisite cellular functions of Hsp90 change with growth temperature. We present here for the first time the results of heterozygous deletion collection screens conducted at the hypothermic stress temperature of 15°C. Extensive bioinformatic analyses were performed on the resulting data in combination with data from homozygous and heterozygous screens previously conducted at normal (30°C) and hyperthermic stress (37°C) growth temperatures. Our resulting meta-analysis uncovered extensive connections between Hsp90 and (1) general transcription, (2) ribosome biogenesis and (3) GTP binding proteins. Predictions from bioinformatic analyses were tested experimentally, supporting a role for Hsp90 in ribosome stability. Importantly, the integrated analysis of the 15°C heterozygous deletion pool screen with previously conducted 30°C and 37°C screens allows for essential genetic targets of Hsp90 to emerge. Altogether, these novel contributions enable a more complete picture of essential Hsp90 functions.http://europepmc.org/articles/PMC3227642?pdf=render |
| spellingShingle | Eric A Franzosa Véronique Albanèse Judith Frydman Yu Xia Amie J McClellan Heterozygous yeast deletion collection screens reveal essential targets of Hsp90. PLoS ONE |
| title | Heterozygous yeast deletion collection screens reveal essential targets of Hsp90. |
| title_full | Heterozygous yeast deletion collection screens reveal essential targets of Hsp90. |
| title_fullStr | Heterozygous yeast deletion collection screens reveal essential targets of Hsp90. |
| title_full_unstemmed | Heterozygous yeast deletion collection screens reveal essential targets of Hsp90. |
| title_short | Heterozygous yeast deletion collection screens reveal essential targets of Hsp90. |
| title_sort | heterozygous yeast deletion collection screens reveal essential targets of hsp90 |
| url | http://europepmc.org/articles/PMC3227642?pdf=render |
| work_keys_str_mv | AT ericafranzosa heterozygousyeastdeletioncollectionscreensrevealessentialtargetsofhsp90 AT veroniquealbanese heterozygousyeastdeletioncollectionscreensrevealessentialtargetsofhsp90 AT judithfrydman heterozygousyeastdeletioncollectionscreensrevealessentialtargetsofhsp90 AT yuxia heterozygousyeastdeletioncollectionscreensrevealessentialtargetsofhsp90 AT amiejmcclellan heterozygousyeastdeletioncollectionscreensrevealessentialtargetsofhsp90 |