Title page for E-project-042805-153626

Project Type MQP

Submission date 2005-04-28

Author
Michael David Hands, BIO

URN E-project-042805-153626

Center Worcester, MA

Sponsor Reid Gilmore

Title Isoforms of OST Subunit STT3

Advisor
Adams, David S., BB

Availability unrestricted

Abstract
Oligosaccharyl Transferase (OST) N-glycosylates nascent polypeptides as they are being translocated into the endoplasmic reticulum (ER). Mammalian OST contains eight subunits, of which STT3 is believed to be the catalytic one. There are two isoforms of STT3, STT3-A and STT3-B, which have different kinetic and substrate recognition properties. Interestingly, it was found that both isoforms are present in cells from a variety of tissues. However, it is unclear if both are needed for proper functioning of OST. RNAi will be used to knockdown expression of one of the isoforms in HEK293 cells to measure differing effects in N-glycosylation of proteins.

Files
MikeHandsMQP.pdf

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Project Type	MQP
Submission date	2005-04-28
Author	Michael David Hands, BIO
URN	E-project-042805-153626
Center	Worcester, MA
Sponsor	Reid Gilmore
Title	Isoforms of OST Subunit STT3
Advisor	Adams, David S., BB
Availability	unrestricted
Abstract Oligosaccharyl Transferase (OST) N-glycosylates nascent polypeptides as they are being translocated into the endoplasmic reticulum (ER). Mammalian OST contains eight subunits, of which STT3 is believed to be the catalytic one. There are two isoforms of STT3, STT3-A and STT3-B, which have different kinetic and substrate recognition properties. Interestingly, it was found that both isoforms are present in cells from a variety of tissues. However, it is unclear if both are needed for proper functioning of OST. RNAi will be used to knockdown expression of one of the isoforms in HEK293 cells to measure differing effects in N-glycosylation of proteins.
Files	MikeHandsMQP.pdf