Memorial University DAI: Characterization of a gene encoding an RNA-binding protein (rbpA) in the cyanobacterium Synechococcus sp. PCC 7942

advanced search

Digital Archives Initiative
Memorial University - Electronic Theses and Dissertations 4

menu off

add document to favorites : add page to favorites : reference url

back to results : previous : next

Search this object:

0 hit(s) :: previous hit : next hit

View:

previous page : next page

Document Description

Title	Characterization of a gene encoding an RNA-binding protein (rbpA) in the cyanobacterium Synechococcus sp. PCC 7942
Author	Belbin, Thomas James, 1967-
Description	Thesis (Ph. D.), Memorial University of Newfoundland, 1999. Biochemistry
Date	1999
Pagination	279 leaves : ill. (some col.)
Subject	Cyanobacteria--Genetics; RNA-protein interactions
Degree	Ph. D.
Degree Grantor	Memorial University of Newfoundland. Dept. of Biochemistry
Discipline	Biochemistry
Language	Eng
Notes	Bibliography: p. 258-279
Abstract	Many species of cyanobacteria possess genes whose products are highly similar to the RNP family of RNA-binding proteins found in eukaryotes. This work describes the characterization of rbpA, one of two RNA-binding protein {rbp) genes now known to exist in the unicellular cyanobacterium Synechococcus sp. PCC 7942. This gene codes for a protein of 107 amino acids. It contains a single RNA Recognition Motif (RRM) as well as an auxiliary domain rich in glycine residues. -- Mutation of the rbpA gene by insertional inactivation using the spectinomycin resistance omega cassette resulted in a temperature-sensitive phenotype with an altered pigment composition when compared with the wild type organism. This phenotype was not observed in a "control mutant", in which the omega cassette was inserted outside of the rbpA gene. Complementation experiments demonstrated that it was possible to rescue the phenotype of the "knock-out" mutant by insertion of a wild type copy of the rbp A gene into a neutral site in the cyanobacterial genome. -- The function of cyanobacterial RNA-binding proteins is not known. A histidine-tagged form of RbpA (HeRbpA) was purified using metal chelate affinity chromatography. RNA binding experiments demonstrated that this protein showed a preference for poly(A), poly(G) and poly(U) RNA but not poly(C). This specificity did not appear to be significantly affected by removal of the auxiliary domain. Overall, work presented here suggests that the RbpA protein may affect content of the phycobilisome components in the photosynthetic apparatus. It also appears to be a protein which is required for growth at lower temperatures.
Type	Text
Format	Image/jpeg; Application/pdf
Source	Paper copy kept in the Centre for Newfoundland Studies, Memorial University Libraries
Local Identifier	a1355294
Rights	The author retains copyright ownership and moral rights in this thesis. Neither the thesis nor substantial extracts from it may be printed or otherwise reproduced without the author's permission.
Collection	Electronic Theses and Dissertations
Scanning Status	Completed
PDF File	(29.94 MB) -- http://collections.mun.ca/PDFs/theses/Belbin_ThomasJ.pdf
CONTENTdm file name	108389.cpd