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A Zelazny

Publications and source records attributed to A Zelazny.

6 recordsLinked to original sources
PubMed1997

The NG domain of the prokaryotic signal recognition particle receptor, FtsY, is fully functional when fused to an unrelated integral membrane polypeptide.

Recent studies have revealed that Escherichia coli possesses an essential targeting system for integral membrane proteins, similar to the mammalian signal recognition particle (SRP) machinery. One essential protein in this system is FtsY, a homologue of the alpha-subunit of the mammalian SRP-receptor (SR-alpha). However, E. coli does not possess a close homologue of the integral membrane protein SR-beta, which anchors SR-alpha to the membrane. Moreover, although FtsY can be found as a peripheral membrane protein, the majority is found soluble in the cytoplasm. In this study, we obtained genetic and biochemical evidence that FtsY must be targeted to the membrane for proper function. We demonstrate that the essential membrane targeting activity of FtsY is mediated by a 198-residue-long acidic N-terminal domain. This domain can be functionally replaced by unrelated integral membrane polypeptides, thus avoiding the need for specific FtsY membrane targeting factors. Therefore, the N terminus of FtsY constitutes an independent domain, which is required only for the targeting of the C-terminal NG domain of FtsY to the membrane.

Animals↗
PubMed1997

Quantitative analysis of the plain radiographic appearance of Ewing's sarcoma of bone.

RATIONALE AND OBJECTIVES: The authors quantitate the radiographic features that distinguish the plain radiographic appearance of Ewing's sarcoma (ES) from other solitary lesions of bone. METHODS: A total of 709 cases of focal bone lesions, including 44 ES, were analyzed according to demographic, anatomic, and plain radiographic features. Vector analysis of groups of features was performed to determine those that are most sensitive and specific for the appearance of ES in contrast with other lesions in the database. RESULTS: In our sample, Ewing's sarcoma is most consistently a medullary-based (91%) lytic (89%) lesion with at least a partially permeative appearance (82%), poorly defined edges (82%), no margination (91%), and a soft-tissue mass (61%). When these lesions occur in long bones, they most commonly are found in the diaphysis (75%) and are proximal more often than distal. Vector analysis suggests that any primary bone lesion without radiographically visible matrix and with either a soft-tissue mass, an appearance of permeative destruction alone or in combination with other patterns of bone destruction is suspect for the diagnosis. This small subset of common features appears to have a high sensitivity (89%) and prevalence (47%) of ES among the lesions meeting these criteria. Limiting the age of the patients to progressively younger age groups increases the specificity but lowers sensitivity. The vector analysis-generated differential diagnoses includes osteosarcoma, giant-cell tumor, lymphoma, and chondrosarcoma. CONCLUSIONS: A relatively specific set of radiographic features can be defined, which will assist in the radiographic diagnosis of ES and improve upon current textbook descriptions.

Adolescent↗
PubMed1996

Biogenesis and topology of integral membrane proteins: characterization of lactose permease-chloramphenicol acetyltransferase hybrids.

Use of beta-lactamase in gene fusions to study membrane protein topology permits exploitation of its biological activity to select for positive (external) hybrids on ampicillin agar plates. When the enzyme is attached to cytoplasmic loops of a membrane protein, it is not secreted and is therefore unable to confer ampicillin resistance. In this study, we examine the use of the cytoplasmic enzyme chloramphenicol acetyltransferase (Cat) as a complement to the use of periplasmic beta-lactamase, in gene fusion studies. This enzyme is responsible for chloramphenicol resistance in Escherichia coli. We show that Cat confers substantial antibiotic resistance when fused to cytoplasmic loops of lactose permease. As expected, periplasmically exposed Cat is enzymatically active in vitro but unable to confer significant chloramphenicol resistance, presumably because of the absence of acetylcoenzyme A in the periplasm. Therefore, Cat may serve as a topogenic sensor in gene fusion studies. The new Cat fusion approach is discussed with regard to its potential use for selecting E. coli mutants which are defective in the assembly of membrane proteins.

Base Sequence↗