Student Work
Investigating the Unusual Gene Structure of DNA Primase in Mycobacteriophage Subclusters
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open in viewerIn A4 and other subclusters of mycobacteriophages, DNA primase is a two-domain protein made from two genes with significant overlap that are read in different open reading frames. These genes create a functioning protein through an unknown mechanism. Our investigations using multiple sequence alignments and protein modelling do not support intein splicing, ribosomal frameshifting, or RNA polymerase slippage as mechanisms of forming a functional\nDNA primase. Preliminary RT-PCR results suggest both domains are transcribed on one transcript.
- This report represents the work of one or more WPI undergraduate students submitted to the faculty as evidence of completion of a degree requirement. WPI routinely publishes these reports on its website without editorial or peer review.
- Creator
- Publisher
- Identifier
- E-project-042319-171703
- Advisor
- Year
- 2019
- Date created
- 2019-04-23
- Resource type
- Major
- Rights statement
Relações
- Em Collection:
Itens
Itens
Miniatura | Título | Acesso | Embargo Release Date | Ações |
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Final_MQP_Paper.pdf | Público | Baixar | ||
Supplementary_Data.zip | Público | Baixar |
Permanent link to this page: https://digital.wpi.edu/show/nc580q656