Unknown

Dataset Information

0

Genome-wide analysis of protein disorder in Arabidopsis thaliana: implications for plant environmental adaptation.


ABSTRACT: Intrinsically disordered proteins/regions (IDPs/IDRs) are currently recognized as a widespread phenomenon having key cellular functions. Still, many aspects of the function of these proteins need to be unveiled. IDPs conformational flexibility allows them to recognize and interact with multiple partners, and confers them larger interaction surfaces that may increase interaction speed. For this reason, molecular interactions mediated by IDPs/IDRs are particularly abundant in certain types of protein interactions, such as those of signaling and cell cycle control. We present the first large-scale study of IDPs in Arabidopsis thaliana, the most widely used model organism in plant biology, in order to get insight into the biological roles of these proteins in plants. The work includes a comparative analysis with the human proteome to highlight the differential use of disorder in both species. Results show that while human proteins are in general more disordered, certain functional classes, mainly related to environmental response, are significantly more enriched in disorder in Arabidopsis. We propose that because plants cannot escape from environmental conditions as animals do, they use disorder as a simple and fast mechanism, independent of transcriptional control, for introducing versatility in the interaction networks underlying these biological processes so that they can quickly adapt and respond to challenging environmental conditions.

SUBMITTER: Pietrosemoli N 

PROVIDER: S-EPMC3567104 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

altmetric image

Publications

Genome-wide analysis of protein disorder in Arabidopsis thaliana: implications for plant environmental adaptation.

Pietrosemoli Natalia N   García-Martín Juan A JA   Solano Roberto R   Pazos Florencio F  

PloS one 20130207 2


Intrinsically disordered proteins/regions (IDPs/IDRs) are currently recognized as a widespread phenomenon having key cellular functions. Still, many aspects of the function of these proteins need to be unveiled. IDPs conformational flexibility allows them to recognize and interact with multiple partners, and confers them larger interaction surfaces that may increase interaction speed. For this reason, molecular interactions mediated by IDPs/IDRs are particularly abundant in certain types of prot  ...[more]

Similar Datasets

| S-EPMC3494268 | biostudies-other
| S-EPMC4463847 | biostudies-other
| S-EPMC2798830 | biostudies-literature
| S-EPMC1188001 | biostudies-literature
| S-EPMC3100966 | biostudies-literature
| S-EPMC8092594 | biostudies-literature
| S-EPMC4232226 | biostudies-literature
| S-EPMC4315298 | biostudies-literature
| S-EPMC1914337 | biostudies-literature
| S-EPMC5623955 | biostudies-literature