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L J Jung

Publications and source records attributed to L J Jung.

6 recordsLinked to original sources
PubMed1995

Candidate genes for the phycoerythrocyanin alpha subunit lyase. Biochemical analysis of pecE and pecF interposon mutants.

The rod substructures of the Anabaena sp. PCC 7120 phycobilisome contain the light harvesting proteins C-phycocyanin and phycoerythrocyanin (PEC). Even at low light intensities, PEC represents no more than 5% of the phycobilisome protein. The beta subunits of both proteins carry thioether-linked phycocyanobilin (PCB) at beta-Cys-82 and beta-Cys-155; however, C-phycocyanin has PCB at alpha-Cys-84 whereas PEC alpha subunit carries phycobiliviolin at this position. The Anabaena sp. PCC 7120 pec operon is made up of five genes. PecB and pecA encode the beta and alpha subunits of PEC, pecC encodes a linker polypeptide associated with PEC in the rod substructure, and pecE and pecF are genes of unknown function that show a high degree of homology to cpcE and cpcF, that encode a C-phycocyanin alpha subunit PCB lyase (Fairchild, C. D., Zhao, J., Zhou, J., Colson, S. E., Bryant, D. A., and Glazer, A. N. (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 7017-7021). Insertional mutants in pecE and pecF, and an interposon mutant in which a portion of both pecE and pecF was deleted, were constructed. All three types of mutants grew 1.3 times slower than wild-type under limiting light conditions and showed a 20% reduction in the PCB content of whole cells relative to chlorophyll alpha. Holo-PEC was missing from the phycobilisomes of all three types of mutants and the level of the PEC linker polypeptide was reduced relative to the wild-type. However, approximately 30% of the wild-type level of the PEC beta subunit was present in all of these phycobilisomes. In contrast, the PEC alpha subunit was barely detectable in the pecE and pecF mutants, but was present in the pecEF deletion mutant as a PCB-adduct in a 1:1 ratio with the PEC beta subunit. The identity of this "unnatural" adduct was confirmed by isolation of the subunit and amino-terminal sequencing. These biochemical results support the inference that pecE and pecF encode a PEC alpha subunit phycobiliviolin lyase, and, in conjunction with earlier findings, demonstrate that phycobiliprotein bilin lyases show high selectivity (rather than absolute specificity) for both the bilin and the polypeptide substrate.

Amino Acid Sequence↗
PubMed1994

Three-dimensional structure in solution of griseoviridin, a group A antibiotic.

The solution conformation of griseoviridin, a broad spectrum antibiotic, has been determined by 1H-NMR in deuterated dimethylsulfoxide. The structural determination is based on experimental data of NOE constraints Five structures were obtained from restrained molecular dynamics calculations, by imposing (the condition for) a minimum violation of distance constraints. These structures satisfy well the experimental restraints, with small values of NOE violation and total energies. On comparison with its crystal structure, a good agreement is noted with a backbone root-mean-square deviation value of 0.084 nm. However, a small variation between the structures is observed at the aminodecanoic acid part of the molecule.

Anti-Bacterial Agents↗
PubMed1994

Solution conformation of enopeptin A, a depsipeptide antibiotic, using 2D NMR and restrained molecular dynamics studies.

Studies on the solution conformation of the cyclic depsipeptide antibiotic enopeptin A have been carried out using 2D NMR and molecular modelling techniques. The proton resonances of the antibiotic in DMSO-d6 have been assigned by the use of TOCSY and ROESY experiments. The interproton distance information obtained from the ROESY experiments have been used as the basis for elucidating the probable structures in solution. The restrained molecular dynamics technique was applied to calculate the structures in solution, and six resultant structures with fewer distance constraint violations were obtained that satisfy the experimental restraints very well. The conformation of the cyclic moiety of the molecules is well defined whereas the aliphatic chain segment is disordered.

Amino Acid Sequence↗
PubMed1993

Expression of mutant ELH prohormones in AtT-20 cells: the relationship between prohormone processing and sorting.

Posttranslational processing of many proteins is essential to the synthesis of fully functional molecules. The ELH (egg-laying hormone) prohormone is cleaved by endoproteases in a specific order at a variety of basic residue processing sites to produce mature peptides. The prohormone is first cleaved at a unique tetrabasic site liberating two intermediates (amino and carboxy) which are sorted to different classes of dense core vesicles in the bag cell neurons of Aplysia. When expressed in AtT-20 cells, the ELH prohormone is also first cleaved at the tetrabasic site. The amino-terminal intermediate is then sorted to the constitutive pathway, and a portion of the carboxy-terminal intermediate is sorted to the regulated pathway. Here, we use mutant constructs of the ELH prohormone expressed in AtT-20 cells to examine the relationship between prohormone processing and consequent sorting. Prohormone which has a dibasic site in place of the tetrabasic site is processed and sorted similarly to wild type. Furthermore, mutant prohormone which lacks the tetrabasic site is processed at an alternative site comprising three basic residues. In these mutant prohormones, mature ELH is still produced and stored in dense core vesicles while amino-terminal products are constitutively secreted. However, deletion of the tetrabasic and tribasic sites results in the rerouting of the amino-terminal intermediate products from the constitutive pathway to the regulated secretory pathway. Thus, in the ELH prohormone, the location of the proteolytic processing events within the secretory pathway and the order of cleavages regulate the sorting of peptide products.

Amino Acid Sequence↗
PubMed1991

Peptide processing and targeting in the neuronal secretory pathway.

The abdominal ganglion of the marine mollusk Aplysia contains a pair of identified neuronal clusters, the bag cells, which control egg laying by means of a number of unique regulatory mechanisms. Each neuron in the bag cell clusters synthesizes several peptides derived from a single prohormone and packages them into separate vesicles. These vesicles are then differentially localized in specific neuronal processes, thus segregating peptides destined for autocrine and hormonal release sites. Therefore in this system, protein trafficking through the secretory pathway organizes multiple peptide neurochemical messengers to efficiently regulate simple behaviors.

Animals↗