Mosley Lab @ IUSM

DEPARTMENT OF BIOCHEMISTRY AND MOLECULAR BIOLOGY

CENTER FOR COMPUTATIONAL BIOLOGY AND BIOINFORMATICS

NEWS

 

  • June 2020 - We are happy to welcome summer research students Josh and Layla!

  • May 2020 - We are happy to welcome Neil (PhD-track) and Sagara (MD-PhD-track) to our team!

  • April 2020 - Congratulations to Sarah on a successful PhD thesis defense!

  • January 2020 - Congratulations to Jose on a successful PhD thesis defense!

Follow us on social media!

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@mosley_lab

OUR LATEST RESEARCH

Hot off the press: Temperature sensitive Mutant Proteome Profiling (TeMPP)

Temperature sensitive Mutant Proteome Profiling (TeMPP) is a novel application of mass spectrometry (MS) based thermal proteome profiling (TPP) to characterize effects of missense mutations on protein stability and protein-protein interactions. This study characterizes missense mutations in two different subunits of the 26S proteasome on the thermal stability of the proteome at large, revealing distinct mechanistic details that were not obtained using only steady-state transcriptome and proteome analyses. Overall, TeMPP is a precise, unbiased approach to rapidly measure changes in missense mutant containing proteomes without the requirement for large amounts of starting material, specific antibodies against proteins of interest, and/or genetic manipulation of the biological system.

Dial-In on how Phosphatase Rtr1 Fine Tunes Transcription Termination

 

The C-terminal domain (CTD) of the largest subunit of RNAPII is dynamically phosphorylated during transcription. The CTD phosphorylation status is critical for the recruitment and interaction of transcription regulatory proteins with RNAPII. In this manuscript, we present data that shows that the CTD phosphatase Rtr1 restricts early termination of RNAPII transcription.

Six degrees of RNA Polymerase II—Interaction Network Building using Mass Spectrometry

 

RNA Polymerase II (RNAPII) is the protein complex responsible for transcribing mRNA and many non-coding RNA. Proper transcription of these RNA is critical to maintaining gene expression and cell health. Consequently, RNAPII interacts with a multitude of other proteins that aid in proper regulation of transcription. This article reviews how mass spectrometry has helped to tease out the intricate and dynamic protein-protein interaction network of RNAPII that is responsible for maintaining transcription. 

Transcription-Coupled RNA Quality Control: A lesson in how to check yourself before you wreck yourself

 

Nascent RNA that are improperly processed or contain transcription errors pose a threat to cell health, and can even cause disease. Fortunately, RNAPII transcriptions are processed for quality control in tandem with transcription. Processing machinery is recruited to RNAPII at the site of transcription and this article reviews these known and emerging co-transcriptional quality control mechanisms.

The Mosley lab

Indiana University School of Medicine

Department of Biochemistry and Molecular Biology

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