UMBC Biological Sciences Department
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With more than 30 tenured and tenure-track faculty members and lecturers, UMBC’s Department of Biological Sciences is one of the university’s largest academic departments encompassing a wide breadth of research and teaching. Research faculty in the Biological Sciences focus on:
- Cell Biology
- Computational Biology
- Developmental Biology & Immunology
- Evolutionary Biology
- Molecular Biology & Genetics
- Neuroscience
- Plant Biology
Recent Submissions
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Mapping of ribosomal protein genes by in vitro protein synthesis using DNA fragments of lambda fus3 transducing phage DNA as templates
(1977-10-25)hfus3 (or hfus2) transducing phage stimulates the synthesis of 27 ribosomal proteins, elongation factors EF-Tu and EF-G, and RNA polymerase subunit (Y in ultraviolet-irradiated Escherichia roli cells (see a preceding ... -
Cluster of genes in Escherichia coli for ribosomal proteins, ribosomal RNA, and RNA polymerase subunits
(National Academy of Sciences, 1975-07-01)This work was supported in part by the College of Agriculture and Life Sciences, University of Wisconsin, and by grants from the National Science Foundation (GB31086) and the National Institute of General Medical Sciences ... -
Specialized transducing phages for ribosomal protein genes of Escherichia coli
(National Academy of Sciences, 1975-01-01)Specialized lambda transducing phages have been isolated carrying approximately half the ribosomal protein genes of E. coli. These phages carry regions of the bacterial chromosome between aroE and fus. The ribosomal protein ... -
The small and large ribosomal subunits depend on each other for stability and accumulation
(Life Science Alliance, 2019-03-05)The 1:1 balance between the numbers of large and small ribosomal subunits can be disturbed by mutations that inhibit the assembly of only one of the subunits. Here, we have investigated if the cell can counteract an imbalance ... -
Analysis of cell cycle parameters during the transition from unhindered growth to ribosomal and translational stress conditions
(PLOS, 2017-10-13)Abrogation of ribosome synthesis (ribosomal stress) leads to cell cycle arrest. However, the immediate cell response to cessation of ribosome formation and the transition from normal cell proliferation to cell cycle arrest ... -
The Ribosomal Protein uL22 Modulates the Shape of the Protein Exit Tunnel
(Cell Press, 2017-08-01)Erythromycin is a clinically useful antibiotic that binds to an rRNA pocket in the ribosomal exit tunnel. Commonly, resistance to erythromycin is acquired by alterations of rRNA nucleotides that interact with the drug. ... -
The extended loops of ribosomal proteins uL4 and uL22 of Escherichia coli contribute to ribosome assembly and protein translation
(Oxford University Press, 2016-06-01)Nearly half of ribosomal proteins are composed of a domain on the ribosome surface and a loop or extension that penetrates into the organelle's RNA core. Our previous work showed that ribosomes lacking the loops of ribosomal ... -
A new system for naming ribosomal proteins
(Elsevier Ltd, 2014-02-10)A system for naming ribosomal proteins is described that the authors intend to use in the future. They urge others to adopt it. The objective is to eliminate the confusion caused by the assignment of identical names to ... -
Repressed synthesis of ribosomal proteins generates protein-specific cell cycle and morphological phenotypes
(American Society for Cell Biology, 2013-10-09)The biogenesis of ribosomes is coordinated with cell growth and proliferation. Distortion of the coordinated synthesis of ribosomal components affects not only ribosome formation, but also cell fate. However, the connection ... -
RNase MRP is required for entry of 35S precursor rRNA into the canonical processing pathway
(The RNA Society, 2009-07)RNase MRP is a nucleolar RNA–protein enzyme that participates in the processing of rRNA during ribosome biogenesis. Previous experiments suggested that RNase MRP makes a nonessential cleavage in the first internal transcribed ... -
Comparative studies on translation arrest in the CrbCmlA and SecM Peptides
(American Society for Microbiology, 2008-06-27)Amino acids are polymerized into peptides in the peptidyl transferase center of the ribosome. The nascent peptides then pass through the exit tunnel before they reach the extraribosomal environment. A number of nascent ... -
Mutation from guanine to adenine in 25S rRNA at the position equivalent to E. coli A2058 does not confer erythromycin sensitivity in Sacchromyces cerevisae
(The RNA Society, 2008-03)The macrolide erythromycin binds to the large subunit of the prokaryotic ribosome near the peptidyltransferase center (PTC) and inhibits elongation of new peptide chains beyond a few amino acids. Nucleotides A2058 and ... -
Regulation of Ribosomal Protein Synthesis in Vibrio cholerae
(American Society for Microbiology, 2004-09)We have investigated the regulation of the S10 and spc ribosomal protein (r-protein) operons in Vibrio cholerae. Both operons are under autogenous control; they are mediated by r-proteins L4 and S8, respectively. Our results ... -
Identification of a functional core in the RNA component of RNase MRP of budding yeasts
(Oxford University Press, 2004-07-14)RNase MRP is an endonuclease participating in ribosomal RNA processing. It consists of one RNA and at least nine protein subunits. Using oligonucleotide-directed mutagenesis, we analyzed the functional role of five of the ... -
The extended loops of ribosomal proteins L4 and L22 are not required for ribosome assembly or L4-mediated autogenous control
(The RNA Society, 2003-10)Ribosomal proteins L4 and L22 both have a globular domain that sits on the surface of the large ribosomal subunit and an extended loop that penetrates its core. The tips of both loops contribute to the lining of the peptide ... -
RNA-structural Mimicry in Escherichia coli Ribosomal Protein L4-dependent Regulation of the S10 Operon
(American Society for Biochemistry and Molecular Biology, 2003-07-25)Ribosomal protein L4 regulates the 11-gene S10 operon in Escherichia coli by acting, in concert with transcription factor NusA, to cause premature transcription termination at a Rho-independent termination site in the ... -
Phylogenetic analysis of the structure of RNase MRP RNA in yeasts
(The RNA Society, 2002-06)RNase MRP is a ribonucleoprotein enzyme involved in processing precursor rRNA in eukaryotes. To facilitate our structure-function analysis of RNase MRP from Saccharomyces cerevisiae, we have determined the likely secondary ... -
Interactions among the protein and RNA subunits of Saccharomyces cerevisiae nuclear RNase P
(National Academy of Sciences, 2002-03-05)Ribonuclease P (RNase P) is a ubiquitous endoribonuclease that cleaves precursor tRNAs to generate mature 5′ termini. Although RNase P from all kingdoms of life have been found to have essential RNA subunits, the number ... -
Surprising flexibility of leader RNA determinants for r-protein L4-mediated transcription termination in the Escherichia coil S10 operon
(The RNA Society, 2002-05)Escherichia coli ribosomal protein L4 autogenously regulates transcription of the S10 operon, which encodes L4 and 10 other ribosomal proteins. Regulation results from L4-stimulated premature transcription termination at ... -
Functional equivalence of hairpins in the RNA subunits of RNase MRP and RNase P in Saccharomyces cerevisiae
(The RNA Society, 2000-05)RNase MRP and RNase P are both ribonucleoprotein enzymes performing endonucleolytic cleavage of RNA. RNase MRP cleaves at a specific site in the precursor-rRNA transcript to initiate processing of the 5.8S rRNA. RNase ...
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