1989
DOI: 10.1007/bf02917437
|View full text |Cite
|
Sign up to set email alerts
|

Incorporation of tellurium into amino acids and proteins in a tellurium-tolerant fungi

Abstract: Aspergillus fumigatus, Aspergillus terreus, and Penicillium chrysogenum, a tellurium tolerant fungi, are able to grow on sulfur free medium amended with 0.2% (w/v) tellurite. Tellurium was incorporated into several types of low and high molecular weight proteins. The newly detected telluro-proteins contained an extraordinary high level of tellurium, as well as telluro-cysteine, telluro-cystine, telluro-methionine, and serine.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

1
38
0

Year Published

1997
1997
2014
2014

Publication Types

Select...
6
3

Relationship

0
9

Authors

Journals

citations
Cited by 76 publications
(40 citation statements)
references
References 14 publications
1
38
0
Order By: Relevance
“…2(d) the longer delay of 34.2 ms optimized for the smaller coupling constant was used to enhance the less sensitive b-protons. Similar results (not shown) were obtained with tellurophene (6), which also has a large and a small coupling constant.…”
Section: Resultssupporting
confidence: 91%
“…2(d) the longer delay of 34.2 ms optimized for the smaller coupling constant was used to enhance the less sensitive b-protons. Similar results (not shown) were obtained with tellurophene (6), which also has a large and a small coupling constant.…”
Section: Resultssupporting
confidence: 91%
“…Indeed there have been reports of sulfur globule formation occurring in several magnetotactic bacteria, although the mechanism is still unknown (3,36). There are literature reports of tellurium substitution of sulfur in amino acids such as cysteine in tellurium-resistant fungi (26,31). Therefore, as tellurium can be considered to be an analogue to sulfur, we tentatively suggest that the tellurium nanorods described in this report are analogues to sulfur globules.…”
Section: Discussionmentioning
confidence: 56%
“…Selenomethionine is then randomly incorporated into proteins due to the editing tolerance of methionyl-tRNA synthetase (10,35). Although the intracellular fate of telluromethionine is less well known, the existence of telluromethionine, methyltelluromethionine, and, to a lesser extent, tellurocysteine has been reported from the cultivation of yeast and bacteria in the presence of high concentrations of Te(IV) (42,71). Telluromethionine has also been shown to be able to replace methionine residues in about 40% of the copies of the protein dihydrofolate reductase in E. coli (3).…”
Section: Discussionmentioning
confidence: 99%